text:
List of winners of the New York City Marathon
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The New York City Marathon is a 42,195-meter (26.2 mile) race through all five boroughs of New York City, and ranks as the largest marathon in the world, with a record 51,392 finishers (29,927 men/21,465 women) in 2016. Since its inaugural race in 1970, 34 men and 25 women have won the open division of the New York City Marathon, representing 22 different countries. From 1970 through 1975, the race was held entirely in Central Park. It has started in Staten Island and gone through New York City's other four boroughs since 1976. Grete Waitz of Norway has won the race more than any other athlete, having completed her 9th victory in 1988, setting three course records in the process. Current course records were set by Geoffrey Mutai of Kenya in 2011 in the men's division, and by Margaret Okayo of Kenya in 2003 in the women's division.
A wheelchair race has been held since 2000. Among the wheelchair racers, Edith Hunkeler of Switzerland and Tatyana McFadden of USA has the most victories, with five each (McFadden has four in a row). Tatyana McFadden also holds the women's course record with a time of 1:43:04 set in 2015, while Kurt Fearnley of Australia holds the men's record with 1:29:22 set in 2006.
Contents
[hide]
1 Men's open division
2 Women's open division
3 Men's wheelchair division
4 Women's wheelchair division
5 Victories by nationality
6 References
7 External links
Men's open division[edit]
Rodgers Rop, winner of the 2002 New York City Marathon. He won the Boston Marathon that same year.
Paul Tergat, winner of the 2005 New York City Marathon, participating in an event for the World Food Program.
Marílson Gomes dos Santos, winner of the 2006 and 2008 New York City Marathons, and the first and only Brazilian to win it in either division.
Year
Winner
Country
Time
Notes
1970 Gary Muhrcke United States 2:31:38 Course record
1971 Norman Higgins United States 2:22:54 Course record
1972 Sheldon Karlin United States 2:27:52
1973 Tom Fleming United States 2:21:54 Course record
1974 Norbert Sander United States 2:26:30
1975 Tom Fleming United States 2:19:27 Course record, 2nd victory
1976 Bill Rodgers United States 2:10:10 Course record
1977 Bill Rodgers United States 2:11:28 2nd victory
1978 Bill Rodgers United States 2:12:12 3rd victory
1979 Bill Rodgers United States 2:11:42 4th victory
1980 Alberto Salazar United States 2:09:41 Course record
1981 Alberto Salazar United States 2:08:13 World record, 2nd victory
1982 Alberto Salazar United States 2:09:29 3rd victory
1983 Rod Dixon New Zealand 2:08:59
1984 Orlando Pizzolato Italy 2:14:53
1985 Orlando Pizzolato Italy 2:11:34 2nd victory
1986 Gianni Poli Italy 2:11:06
1987 Ibrahim Hussein Kenya 2:11:01
1988 Steve Jones United Kingdom 2:08:20
1989 Juma Ikangaa Tanzania 2:08:01 Course record
1990 Douglas Wakiihuri Kenya 2:12:39
1991 Salvador García Mexico 2:09:28
1992 Willie Mtolo South Africa 2:09:29
1993 Andrés Espinosa Mexico 2:10:04
1994 Germán Silva Mexico 2:11:21
1995 Germán Silva Mexico 2:11:00 2nd victory
1996 Giacomo Leone Italy 2:09:54
1997 John Kagwe Kenya 2:08:12
1998 John Kagwe Kenya 2:08:45 2nd victory
1999 Joseph Chebet Kenya 2:09:14
2000 Abdelkader El Mouaziz Morocco 2:10:09
2001 Tesfaye Jifar Ethiopia 2:07:43 Course record
2002 Rodgers Rop Kenya 2:08:07
2003 Martin Lel Kenya 2:10:30
2004 Hendrick Ramaala South Africa 2:09:28
2005 Paul Tergat Kenya 2:09:30
2006 Marílson Gomes dos Santos Brazil 2:09:58
2007 Martin Lel Kenya 2:09:04 2nd victory
2008 Marílson Gomes dos Santos Brazil 2:08:43 2nd victory
2009 Meb Keflezighi United States 2:09:15
2010 Gebregziabher Gebremariam Ethiopia 2:08:14
2011 Geoffrey Mutai Kenya 2:05:06 Course record
2012 Cancelled due to Hurricane Sandy
2013 Geoffrey Mutai Kenya 2:08:24 2nd victory
2014 Wilson Kipsang Kenya 2:10:59
2015 Stanley Biwott Kenya 2:10:34
2016 Ghirmay Ghebreslassie Eritrea 2:07:51
2017 Geoffrey Kamworor Kenya 2:10:53
Women's open division[edit]
Paula Radcliffe, winner of the 2004, 2007 & 2008 New York City Marathons.
Jeļena Prokopčuka, winner of the 2005 and 2006 New York City Marathons, the first and only Latvian runner to win in either division.
Year
Winner
Country
Time
Notes
1972 Nina Kuscsik United States 3:08:41 Course record
1973 Nina Kuscsik United States 2:57:07 Course record, 2nd victory
1974 Kathrine Switzer United States 3:07:29
1975 Kim Merritt United States 2:46:14 Course record
1976 Miki Gorman United States 2:39:11 Course record
1977 Miki Gorman United States 2:43:10 2nd victory
1978 Grete Waitz Norway 2:32:30 Course record
1979 Grete Waitz Norway 2:27:33 Course record, 2nd victory
1980 Grete Waitz Norway 2:25:42 Course record, 3rd victory
1981 Allison Roe New Zealand 2:25:29 Course record
1982 Grete Waitz Norway 2:27:14 4th victory
1983 Grete Waitz Norway 2:27:00 5th victory
1984 Grete Waitz Norway 2:29:30 6th victory
1985 Grete Waitz Norway 2:28:34 7th victory
1986 Grete Waitz Norway 2:28:06 8th victory
1987 Priscilla Welch United Kingdom 2:30:17
1988 Grete Waitz Norway 2:28:07 9th victory
1989 Ingrid Kristiansen Norway 2:25:30
1990 Wanda Panfil Poland 2:30:45
1991 Liz McColgan United Kingdom 2:27:32
1992 Lisa Ondieki Australia 2:24:40 Course record
1993 Uta Pippig Germany 2:26:24
1994 Tegla Loroupe Kenya 2:27:37
1995 Tegla Loroupe Kenya 2:28:06 2nd victory
1996 Anuţa Cătună Romania 2:28:18
1997 Franziska Rochat-Moser Switzerland 2:28:43
1998 Franca Fiacconi Italy 2:25:17
1999 Adriana Fernandez Mexico 2:25:06
2000 Lyudmila Petrova Russia 2:25:45
2001 Margaret Okayo Kenya 2:24:21 Course record
2002 Joyce Chepchumba Kenya 2:25:56
2003 Margaret Okayo Kenya 2:22:31 Course record, 2nd victory
2004 Paula Radcliffe United Kingdom 2:23:10
2005 Jeļena Prokopčuka Latvia 2:24:41
2006 Jeļena Prokopčuka Latvia 2:25:05 2nd victory
2007 Paula Radcliffe United Kingdom 2:23:09 2nd victory
2008 Paula Radcliffe United Kingdom 2:23:56 3rd victory
2009 Derartu Tulu Ethiopia 2:28:52
2010 Edna Kiplagat Kenya 2:28:20
2011 Firehiwot Dado Ethiopia 2:23:15
2012 Cancelled due to Hurricane Sandy
2013 Priscah Jeptoo Kenya 2:25:07
2014 Mary Keitany Kenya 2:25:07
2015 Mary Keitany Kenya 2:24:25 2nd victory
2016 Mary Keitany Kenya 2:24:26 3rd victory
2017 Shalane Flanagan United States 2:26:53 Fifth US woman to win; first since 1977
Men's wheelchair division[edit]
David Weir, winner of the 2010 race
Masazumi Soejima, winner of the 2011 race
Year
Winner
Country
Time
Notes
2000 Ayari, KamelKamel Ayari Tunisia 1:53:50 [1]
2001 Mendoza, SaúlSaúl Mendoza Mexico 1:39:29 Course record[2]
2002 Schabort, KrigeKrige Schabort South Africa 1:38:27 Course record[3]
2003 Schabort, KrigeKrige Schabort South Africa 1:32:19 Course record, 2nd victory[4]
2004 Mendoza, SaúlSaúl Mendoza Mexico 1:33:16 2nd victory[5]
2005 van Dyk, ErnstErnst van Dyk South Africa 1:31:11 Course record[6]
2006 Fearnley, KurtKurt Fearnley Australia 1:29:22 Course record[7]
2007 Fearnley, KurtKurt Fearnley Australia 1:33:58 2nd victory[8]
2008 Fearnley, KurtKurt Fearnley Australia 1:44:51 3rd victory[9]
2009 Fearnley, KurtKurt Fearnley Australia 1:35:58 4th victory
2010 Weir, DavidDavid Weir United Kingdom 1:37:29
2011 Soejima, MasazumiMasazumi Soejima Japan 1:31:41
2012 Cancelled due to Hurricane Sandy
2013 Hug, MarcelMarcel Hug Switzerland 1:40:14
2014 Fearnley, KurtKurt Fearnley Australia 1:30:55 5th victory (Note that the course was shortened by 3 miles at the start)
2015 van Dyk, ErnstErnst van Dyk South Africa 1:30:54 2nd victory
2016 Hug, MarcelMarcel Hug Switzerland 1:35:44 2nd victory
2017 Hug, MarcelMarcel Hug Switzerland 1:37.17 3rd victory
Women's wheelchair division[edit]
Year
Winner
Country
Time
Notes
2000 Xuan, Anh Nguyen ThiAnh Nguyen Thi Xuan Vietnam 2:46:47 [1]
2001 Porcellato, FrancescaFrancesca Porcellato Italy 2:08:51 Course record[10]
2002 Blauwet, CheriCheri Blauwet United States 2:14:39 [3]
2003 Blauwet, CheriCheri Blauwet United States 1:59:30 Course record, 2nd victory[4]
2004 Hunkeler, EdithEdith Hunkeler Switzerland 1:53:27 Course record[5]
2005 Hunkeler, EdithEdith Hunkeler Switzerland 1:54:52 2nd victory[6]
2006 McGrory, AmandaAmanda McGrory United States 1:54:19 2 seconds ahead of 2nd-place finisher[7]
2007 Hunkeler, EdithEdith Hunkeler Switzerland 1:52:38 Course record, 3rd victory[8]
2008 Hunkeler, EdithEdith Hunkeler Switzerland 2:06:42 4th victory[9]
2009 Hunkeler, EdithEdith Hunkeler Switzerland 1:58:15 5th victory
2010 McFadden, TatyanaTatyana McFadden United States 2:02:22
2011 McGrory, AmandaAmanda McGrory United States 1:50:25 Course record
2012 Cancelled due to Hurricane Sandy
2013 McFadden, TatyanaTatyana McFadden United States 1:59:13 2nd victory
2014 McFadden, TatyanaTatyana McFadden United States 1:42:16 3rd victory (Note that their course was shortened by 3 miles at the start)
2015 McFadden, TatyanaTatyana McFadden United States 1:43:04 4th victory; course record
2016 McFadden, TatyanaTatyana McFadden United States 1:47:43 5th victory
Victories by nationality[edit]
Country
Men's
Open
Women's
Open
Men's
Wheelchair
Women's
Wheelchair
Total
United States 14 7 0 9 30
Kenya 14 10 0 0 24
Norway 0 10 0 0 10
Mexico 4 1 2 0 7
United Kingdom 1 5 1 0 7
Switzerland 0 1 3 5 9
Italy 4 1 0 1 6
Australia 0 1 5 0 6
South Africa 2 0 4 0 6
Ethiopia 2 2 0 0 4
Brazil 2 0 0 0 2
New Zealand 1 1 0 0 2
Latvia 0 2 0 0 2
Morocco 1 0 0 0 1
Tanzania 1 0 0 0 1
Germany 0 1 0 0 1
Poland 0 1 0 0 1
Romania 0 1 0 0 1
Russia 0 1 0 0 1
Tunisia 0 0 1 0 1
Vietnam 0 0 0 1 1
Eritrea 1 0 0 0 1
References[edit]
^ Jump up to: a b Dicker, Ron (November 6, 2000). "NEW YORK CITY MARATHON: WHEELCHAIRS; In First Official Race, the Winner Stays Clear of Controversy". The New York Times. Retrieved 2009-05-20.
Jump up ^ Rose, Derek; Bill Hutchinson (November 5, 2001). "PATRIOTIC STRUT TO MARATHON". Daily News. Retrieved 2009-05-20. [permanent dead link]
^ Jump up to: a b Lichtenstein, Grace (November 4, 2002). "THE MARATHON: WHEELCHAIR COMPETITION; Swiss Legislator Wins Without Vote". The New York Times. Retrieved 2009-05-20.
^ Jump up to: a b Williams, Lena (November 3, 2003). "Glue and Cable Wire Aid Tenacious Winner". The New York Times. Archived from the original on January 31, 2013. Retrieved 2009-05-20.
^ Jump up to: a b Williams, Lena (November 8, 2004). "MARATHON 2004: NOTEBOOK; Strategy Pays Off in Men's Wheelchair Race". The New York Times. Retrieved 2009-05-20.
^ Jump up to: a b Litsky, Frank (November 7, 2005). "After a Bumpy Challenge, a Road Record and Sore Arms". The New York Times. Retrieved 2009-05-20.
^ Jump up to: a b Litsky, Frank (November 5, 2006). "Potholes Fail to Stop Winner of Wheelchair Race". The New York Times. Retrieved 2009-05-20.
^ Jump up to: a b Litsky, Frank (November 5, 2007). "Racecar Driver Is Fourth in Handcycle". The New York Times. Retrieved 2009-05-20.
^ Jump up to: a b "Defending Champions at New York Marathon". International Paralympic Committee. November 11, 2008. Retrieved 2009-05-20.
Jump up ^ Lilly, Brandon (November 5, 2001). "MARATHON 2001: WHEELCHAIR DIVISION; Israeli Sets Mark in Men's Hand-Cycle Competition". The New York Times. Retrieved 2009-05-20.
External links[edit]
"TCS New York City Marathon Results Archive", New York Road Runners.
"RRIC Annual Marathon Report 2006", Running USA Wire, May 20, 2006.
"New York City Marathon Winners". Encarta. MSN. Archived from the original on 2009-11-01. Retrieved 2008-01-22.
[show]
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New York City Marathon
...1987...
...2010
2011
2012
2013
2014
2015
2016
2017
List of winners
[show]
v
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e
New York City Marathon – men's winners
1970: Gary Muhrcke (USA)
1971: Norman Higgins (USA)
1972: Sheldon Karlin (USA)
1973: Tom Fleming (USA)
1974: Norbert Sander (USA)
1975: Tom Fleming (USA)
1976-79: Bill Rodgers (USA)
1980-82: Alberto Salazar (USA)
1983: Rod Dixon (NZL)
1984-85: Orlando Pizzolato (ITA)
1986: Gianni Poli (ITA)
1987: Ibrahim Hussein (KEN)
1988: Steve Jones (GBR)
1989: Juma Ikangaa (TAN)
1990: Douglas Wakiihuri (KEN)
1991: Salvador García (MEX)
1992: Willie Mtolo (RSA)
1993: Andrés Espinosa (MEX)
1994-95: Germán Silva (MEX)
1996: Giacomo Leone (ITA)
1997-98: John Kagwe (KEN)
1999: Joseph Chebet (KEN)
2000: Abdelkader El Mouaziz (MAR)
2001: Tesfaye Jifar (ETH)
2002: Rodgers Rop (KEN)
2003: Martin Lel (KEN)
2004: Hendrick Ramaala (RSA)
2005: Paul Tergat (KEN)
2006: Marílson Gomes dos Santos (BRA)
2007: Martin Lel (KEN)
2008: Marílson Gomes dos Santos (BRA)
2009: Meb Keflezighi (USA)
2010: Gebregziabher Gebremariam (ETH)
2011: Geoffrey Mutai (KEN)
2012: Marathon canceled
2013: Geoffrey Mutai (KEN)
2014: Wilson Kipsang Kiprotich (KEN)
2015: Stanley Biwott (KEN)
2016: Ghirmay Ghebreslassie (ERI)
2017: Geoffrey Kamworor (KEN)
World Marathon Majors
Berlin Marathon – List (M/W)
Boston Marathon – List (M/W)
Chicago Marathon – List (M/W)
London Marathon – List (M/W)
New York City Marathon – List (M/W)
Tokyo Marathon – List (M/W)
[show]
v
t
e
New York City Marathon – women's winners
1971: Beth Bonner (USA)
1972–1973: Nina Kuscsik (USA)
1974: Kathrine Switzer (USA)
1975: Kim Merritt (USA)
1976–1977: Miki Gorman (USA)
1978–1980: Grete Waitz (NOR)
1981: Allison Roe (NZL)
1982–1986: Grete Waitz (NOR)
1987: Priscilla Welch (GBR)
1988: Grete Waitz (NOR)
1989: Ingrid Kristiansen (NOR)
1990: Wanda Panfil (POL)
1991: Liz McColgan (GBR)
1992: Lisa Ondieki (AUS)
1993: Uta Pippig (GER)
1994–1995: Tegla Loroupe (KEN)
1996: Anuța Cătună (ROM)
1997: Franziska Rochat-Moser (SUI)
1998: Franca Fiacconi (ITA)
1999: Adriana Fernández (MEX)
2000: Lyudmila Petrova (RUS)
2001: Margaret Okayo (KEN)
2002: Joyce Chepchumba (KEN)
2003: Margaret Okayo (KEN)
2004: Paula Radcliffe (GBR)
2005–2006: Jeļena Prokopčuka (LAT)
2007–2008: Paula Radcliffe (GBR)
2009: Derartu Tulu (ETH)
2010: Edna Kiplagat (KEN)
2011: Firehiwot Dado (ETH)
2012: Marathon canceled
2013: Priscah Jeptoo (KEN)
2014–2016: Mary Keitany (KEN)
2017: Shalane Flanagan (USA)
World Marathon Majors
Berlin Marathon – List (M/W)
Boston Marathon – List (M/W)
Chicago Marathon – List (M/W)
London Marathon – List (M/W)
New York City Marathon – List (M/W)
Tokyo Marathon – List (M/W)
[show]
v
t
e
World Marathon Majors
Marathons
Tokyo
winners
Boston
winners
London
winners
Berlin
winners
Chicago
winners
New York City
winners
Results
Final standings
IAAF World Championships Marathon
World Marathon Cup
Olympic Games Marathon
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Margaret Avery
From Wikipedia, the free encyclopedia
Jump to: navigation, search
Margaret Avery
Born
January 20, 1944
Mangum, Oklahoma, United States
Residence
Los Angeles, California
Occupation
Actress
Years active
1972–present
Spouse(s)
Robert Gordon Hunt (1974–1980)
Children
1
Margaret Avery (born January 20, 1944) is an American actress and singer. She began her career appearing on stage and later has had starring roles in films include Cool Breeze (1972), Which Way Is Up? (1977), Scott Joplin (1977), and The Fish That Saved Pittsburgh (1979).
Avery is best known for her performance as Shug Avery in the 1985 period drama film The Color Purple for which she was nominated for an Academy Award for Best Actress in a Supporting Role.[1] She continued appearing in films include Blueberry Hill (1988), White Man's Burden (1995), Welcome Home Roscoe Jenkins (2008), Meet the Browns (2008), and Proud Mary (2018). In 2013, Avery began starring as Helen Patterson, lead character's mother, in the BET drama series Being Mary Jane.
Contents
[hide]
1 Early life
2 Career
3 Personal life
4 Filmography
4.1 Film
4.2 Television
5 References
6 External links
Early life[edit]
Margaret Avery was born in Mangum, Oklahoma and raised in San Diego, California, where she attended Point Loma High School.[2] She then attended San Francisco State University, where in 1985, she earned her degree in education.[3] While working as a substitute teacher in Los Angeles, Avery began making singing and acting appearances.[2]
Career[edit]
Avery is best known for her role as Shug Avery in the 1985 film The Color Purple. Her performance in this screen adaptation of Alice Walker's prize-winning novel The Color Purple earned Avery an Oscar nomination for Best Supporting Actress.
Among the plays Avery appeared in were Revolution and The Sistuhs. In 1972 for her performance in Does a Tiger Wear a Necktie?, she received the Los Angeles Drama Critics Circle Award for Outstanding Performance by an Actress.[4][5]
In the television movie Something Evil (1972), a horror story with Sandy Dennis and Darren McGavin, Avery was directed by Steven Spielberg. That same year she made her theatrical motion picture debut as Lark in the crime film Cool Breeze with Thalmus Rasulala and Judy Pace. In this blaxploitation remake of The Asphalt Jungle, Avery played the Marilyn Monroe part. The following year she played a prostitute in Magnum Force, the second in the series of Dirty Harry films starring Clint Eastwood, in which her character was murdered by her pimp. The character was killed through the pouring drain cleaner down the victim's throat which was said to have inspired the notorious Hi-Fi Murders case in 1974.[6][7]
In the 1977 film Which Way Is Up?, directed by Michael Schultz, Avery gave a comedic performance as Annie Mae, the wife of Richard Pryor's character. That same year, she played Belle Joplin, wife of the ragtime composer Scott Joplin, opposite Billy Dee Williams in the title role.
In 1992 Avery starred in The Jacksons: An American Dream as Martha Scruse, mother of Katherine Jackson, who was played by Angela Bassett.
She has also made guest appearances on TV, including The New Dick Van Dyke Show, Kojak, Sanford and Son, Kolchak: The Night Stalker, A.E.S. Hudson Street, Murder, She Wrote, Miami Vice, Spenser: For Hire, The Cosby Show, Walker, Texas Ranger, and JAG.
In 2008, Avery played Mama Jenkins in Welcome Home Roscoe Jenkins, opposite Martin Lawrence and James Earl Jones, and Sarah Brown in Tyler Perry's Meet the Browns, which also stars Angela Bassett.
Currently, Avery plays recurring character Helen Patterson in BET's series Being Mary Jane.[8]
Personal life[edit]
In January 1974, Margaret Avery married Robert Gordon Hunt. They have one daughter, Aisha Hunt, and divorced in 1980.[2]
Margaret Avery lives in Los Angeles, and remains active in the show business. While continuing to act, she also works with at-risk teenagers and battered women of Greater Los Angeles Area.
Filmography[edit]
Film[edit]
Year
Title
Role
Notes
1972 Something Evil Irene
1972 Cool Breeze Lark
1972 Terror House Edwina
1973 An Eye for an Eye Nurse
1973 Magnum Force Prostitute
1973 An Eye for an Eye Nurse
1973 Hell Up in Harlem Sister Jennifer
1976 Louis Armstrong - Chicago Style Alma Rae NAACP Image Award for Outstanding Actress in a Television Movie, Mini-Series or Dramatic Special
1977 Which Way Is Up? Annie Mae
1977 Scott Joplin Belle Joplin Nominated — NAACP Image Award for Outstanding Actress in a Motion Picture
1979 Fish That Saved Pittsburgh, TheThe Fish That Saved Pittsburgh Toby Millman
1980 Sky Is Gray, TheThe Sky Is Gray Rosemary
1980 Lathe of Heaven, TheThe Lathe of Heaven Heather LeLache
1985 Color Purple, TheThe Color Purple Shug Avery Nominated—Academy Award for Best Supporting Actress
1988 Blueberry Hill Hattie Cale
1989 Riverbend Bell Coleman
1989 Single Women Married Men Grace Williams
1990 Heat Wave Roxie Turpin
1990 Return of Superfly, TheThe Return of Superfly Francine
1993 Lightning in a Bottle Dr. Sierheed
1993 Night Trap Miss Sadie
1994 Cyborg 3: The Recycler Doc Edford
1995 Set-Up, TheThe Set-Up Olivia Dubois
1995 White Man's Burden Megan Thomas
1998 Love Kills Moon
2002 Waitin' to Live Pearline Loggins
2002 Second to Die Insurance agent
2007 Lord Help Us Dorinda Thomas
2007 Exodus Robbed Tourist
2008 Welcome Home Roscoe Jenkins Mama Jenkins
2008 Meet the Browns Sarah Brown
2009 Extrospection Anna
2018 Proud Mary[9] Mary's mother
Television[edit]
Year
Title
Role
Notes
1973 The New Dick Van Dyke Show Pam Harris / Nurse Wilkinson Episode: "What Your Best Friend Doesn't Know"
1973 Ironside' Bartender Episode: "The Last Payment"
1974 Kojak Lula Episode: "You Can't Tell a Hurt Man How to Holler"
1974 Marcus Welby, M.D. Julie Episode: "The 266 Days"
1975 Sanford and Son Denise Episode: "Strange Bedfellows"
1975 Kolchak: The Night Stalker Ruth Van Galen Episode: "The Sentry"
1982 The Powers of Matthew Star April Episode: "Accused"
1983 For Us, the Living Dottie
1987 Rags to Riches Celia Richards (Cee Cee Smith)
1987 Miami Vice Sally Cordova Episode: "The Afternoon Plane"
1992 Jacksons: An American Dream, TheThe Jacksons: An American Dream Martha Scruse
1992 The Cosby Show Leah
1998 Wie stark muss eine Liebe sein Mary McMillian German TV
2012 Single Ladies Josephine Episode: "Ex Factor"
2013–present Being Mary Jane Helen Patterson Recurring Role
References[edit]
Jump up ^ "Actress Gains Visibility, Respect With `Purple`". Sun Sentinel. Retrieved 2010-12-04.
^ Jump up to: a b c Brumburgh, Gary. "IMDb Mini Biography".
Jump up ^ "Celebrate SF State and its extraordinary alumni". San Francisco State University. September 2014.
Jump up ^ O'Donnell, Owen; Steen, Sara (1990). "Contemporary Theatre, Film and Television". Gale. p. 27.
Jump up ^ Los Angeles Times, March 20, 1974, "27 Win Critics' Circle Honors," p. E 1.
Jump up ^ Kinder, Gary (1982). Victim: The Other Side of Murder. Delacorte Press. ISBN 0385291051.
Jump up ^ Douglas, John E., and Olshaker, Mark (1999). The Anatomy of Motive: The FBI's Legendary Mindhunter Explores the Key to Understanding and Catching Violent Criminals. New York: Scribner. pp. 91–109. ISBN 978-0-684-84598-2. CS1 maint: Multiple names: authors list (link)
Jump up ^ "Being Mary Jane". IMDB.
Jump up ^ N'Duka, Amanda (5 April 2017). "Margaret Avery, Xander Berkeley & More Join Taraji P. Henson In 'Proud Mary'". Retrieved 9 July 2017.
External links[edit]
Margaret Avery on IMDb
Margaret Avery at AllMovie
Margaret Avery[permanent dead link] at TV.com
Authority control
WorldCat Identities
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LCCN: n85151555
ISNI: 0000 0000 7730 2657
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SUDOC: 068872615
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SNAC: w64p1z6m
Retrieved from "https://en.wikipedia.org/w/index.php?title=Margaret_Avery&oldid=833293669"
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Protein structure
From Wikipedia, the free encyclopedia
Jump to: navigation, search
Interactive diagram of protein structure, using PCNA as an example. (PDB: 1AXC)
Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, the monomers of the polymer. A single amino acid monomer may also be called a residue indicating a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond. By convention, a chain under 30 amino acids is often identified as a peptide, rather than a protein.[1] To be able to perform their biological function, proteins fold into one or more specific spatial conformations driven by a number of non-covalent interactions such as hydrogen bonding, ionic interactions, Van der Waals forces, and hydrophobic packing. To understand the functions of proteins at a molecular level, it is often necessary to determine their three-dimensional structure. This is the topic of the scientific field of structural biology, which employs techniques such as X-ray crystallography, NMR spectroscopy, and dual polarisation interferometry to determine the structure of proteins.
Protein structures range in size from tens to several thousand amino acids.[2] By physical size, proteins are classified as nanoparticles, between 1–100 nm. Very large aggregates can be formed from protein subunits. For example, many thousands of actin molecules assemble into a microfilament.
A protein generally undergo reversible structural changes in performing its biological function. The alternative structures of the same protein are referred to as different conformational isomers, or simply, conformations, and transitions between them are called conformational changes.
Contents
[hide]
1 Levels of protein structure
1.1 Primary structure
1.2 Secondary structure
1.3 Tertiary structure
1.4 Quaternary structure
2 Domains, motifs, and folds in protein structure
2.1 Structural domain
2.2 Structural and sequence motif
2.3 Supersecondary structure
2.4 Protein fold
2.5 Superdomain
3 Protein folding
4 Protein structure determination
4.1 Protein Sequence Analysis: Ensembles
5 Protein structure databases
6 Structure classification
7 Computational prediction of protein structure
8 See also
9 References
10 Further reading
Levels of protein structure[edit]
There are four distinct levels of protein structure.
Primary structure[edit]
Main article: Protein primary structure
The primary structure of a protein refers to the sequence of amino acids in the polypeptide chain. The primary structure is held together by peptide bonds that are made during the process of protein biosynthesis. The two ends of the polypeptide chain are referred to as the carboxyl terminus (C-terminus) and the amino terminus (N-terminus) based on the nature of the free group on each extremity. Counting of residues always starts at the N-terminal end (NH2-group), which is the end where the amino group is not involved in a peptide bond. The primary structure of a protein is determined by the gene corresponding to the protein. A specific sequence of nucleotides in DNA is transcribed into mRNA, which is read by the ribosome in a process called translation. The sequence of amino acids in insulin was discovered by Frederick Sanger, establishing that proteins have defining amino acid sequences.[3][4] The sequence of a protein is unique to that protein, and defines the structure and function of the protein. The sequence of a protein can be determined by methods such as Edman degradation or tandem mass spectrometry. Often, however, it is read directly from the sequence of the gene using the genetic code. It is strictly recommended to use the words "amino acid residues" when discussing proteins because when a peptide bond is formed, a water molecule is lost, and therefore proteins are made up of amino acid residues. Post-translational modification such as disulfide bond formation, phosphorylations and glycosylations are usually also considered a part of the primary structure, and cannot be read from the gene. For example, insulin is composed of 51 amino acids in 2 chains. One chain has 31 amino acids, and the other has 20 amino acids.
Secondary structure[edit]
An α-helix with hydrogen bonds (yellow dots)
Main article: Protein secondary structure
Secondary structure refers to highly regular local sub-structures on the actual polypeptide backbone chain. Two main types of secondary structure, the α-helix and the β-strand or β-sheets, were suggested in 1951 by Linus Pauling and coworkers.[5] These secondary structures are defined by patterns of hydrogen bonds between the main-chain peptide groups. They have a regular geometry, being constrained to specific values of the dihedral angles ψ and φ on the Ramachandran plot. Both the α-helix and the β-sheet represent a way of saturating all the hydrogen bond donors and acceptors in the peptide backbone. Some parts of the protein are ordered but do not form any regular structures. They should not be confused with random coil, an unfolded polypeptide chain lacking any fixed three-dimensional structure. Several sequential secondary structures may form a "supersecondary unit".[6]
Tertiary structure[edit]
Main article: Protein tertiary structure
Tertiary structure refers to the three-dimensional structure of monomeric and multimeric protein molecules. The α-helixes and β-pleated-sheets are folded into a compact globular structure. The folding is driven by the non-specific hydrophobic interactions, the burial of hydrophobic residues from water, but the structure is stable only when the parts of a protein domain are locked into place by specific tertiary interactions, such as salt bridges, hydrogen bonds, and the tight packing of side chains and disulfide bonds. The disulfide bonds are extremely rare in cytosolic proteins, since the cytosol (intracellular fluid) is generally a reducing environment.
Quaternary structure[edit]
Main article: Protein quaternary structure
Quaternary structure is the three-dimensional structure consisting of the aggregation of two or more individual polypeptide chains (subunits) that operate as a single functional unit. In this context, the quaternary structure is stabilized by the same non-covalent interactions and disulfide bonds as the tertiary structure. Complexes of two or more polypeptides (i.e. multiple subunits) are called multimers. Specifically it would be called a dimer if it contains two subunits, a trimer if it contains three subunits, a tetramer if it contains four subunits, and a pentamer if it contains five subunits. The subunits are frequently related to one another by symmetry operations, such as a 2-fold axis in a dimer. Multimers made up of identical subunits are referred to with a prefix of "homo-" (e.g. a homotetramer) and those made up of different subunits are referred to with a prefix of "hetero-", for example, a heterotetramer, such as the two alpha and two beta chains of hemoglobin.
Domains, motifs, and folds in protein structure[edit]
Protein domains. The two shown protein structures share a common domain (maroon), the PH domain, which is involved in phosphatidylinositol (3,4,5)-trisphosphate binding
Proteins are frequently described as consisting of several structural units. These units include domains, motifs, and folds. Despite the fact that there are about 100,000 different proteins expressed in eukaryotic systems, there are many fewer different domains, structural motifs and folds.
Structural domain[edit]
A structural domain is an element of the protein's overall structure that is self-stabilizing and often folds independently of the rest of the protein chain. Many domains are not unique to the protein products of one gene or one gene family but instead appear in a variety of proteins. Domains often are named and singled out because they figure prominently in the biological function of the protein they belong to; for example, the "calcium-binding domain of calmodulin". Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimera proteins.
Structural and sequence motif[edit]
The structural and sequence motifs refer to short segments of protein three-dimensional structure or amino acid sequence that were found in a large number of different proteins.
Supersecondary structure[edit]
The supersecondary structure refers to a specific combination of secondary structure elements, such as β-α-β units or a helix-turn-helix motif. Some of them may be also referred to as structural motifs.
Protein fold[edit]
A protein fold refers to the general protein architecture, like a helix bundle, β-barrel, Rossman fold or different "folds" provided in the Structural Classification of Proteins database.[7] A related concept is protein topology that refers to the arrangement of contacts within the protein.
Superdomain[edit]
A superdomain consists of two or more nominally unrelated structural domains that are inherited as a single unit and occur in different proteins.[8] An example is provided by the protein tyrosine phosphatase domain and C2 domain pair in PTEN, several tensin proteins, auxilin and proteins in plants and fungi. The PTP-C2 superdomain evidently came into existence prior to the divergence of fungi, plants and animals is therefore likely to be about 1.5 billion years old.
Protein folding[edit]
Main article: Protein folding
Once translated by a ribosome, each polypeptide folds into its characteristic three-dimensional structure from a random coil.[9] Since the fold is maintained by a network of interactions between amino acids in the polypeptide, the native state of the protein chain is determined by the amino acid sequence (Anfinsen's dogma).[10]
Protein structure determination[edit]
Examples of protein structures from the PDB
Rate of Protein Structure Determination by Method and Year
Around 90% of the protein structures available in the Protein Data Bank have been determined by X-ray crystallography.[11] This method allows one to measure the three-dimensional (3-D) density distribution of electrons in the protein, in the crystallized state, and thereby infer the 3-D coordinates of all the atoms to be determined to a certain resolution. Roughly 9% of the known protein structures have been obtained by nuclear magnetic resonance (NMR) techniques.[citation needed] For larger protein complexes, cryo-electron microscopy can determine protein structures. The resolution is typically lower than that of X-ray crystallography, or NMR, but the maximum resolution is steadily increasing. This technique is still a particularly valuable for very large protein complexes such as virus coat proteins and amyloid fibers.
General secondary structure composition can be determined via circular dichroism. Vibrational spectroscopy can also be used to characterize the conformation of peptides, polypeptides, and proteins.[12] Two-dimensional infrared spectroscopy has become a valuable method to investigate the structures of flexible peptides and proteins that cannot be studied with other methods.[13][14] A more qualitative picture of protein structure is often obtained by proteolysis, which is also useful to screen for more crystallizable protein samples. Novel implementations of this approach, including fast parallel proteolysis (FASTpp), can probe the structured fraction and its stability without the need for purification.[15] Once a protein's structure has been experimentally determined, further detailed studies can be done computationally, using molecular dynamic simulations of that structure.[16]
Protein Sequence Analysis: Ensembles[edit]
Schematic view of the two main ensemble modeling approaches.[17]
Proteins are often thought of as relatively stable structures that have a set tertiary structure and experience conformational changes as a result of being modified by other proteins or as part of enzymatic activity. However proteins have varying degrees of stability and some of the less stable variants are intrinsically disordered proteins. These proteins exist and function in a relatively 'disordered' state lacking a stable tertiary structure. As a result, they are difficult to describe in a standard protein structure model that was designed for proteins with a fixed tertiary structure. Conformational ensembles have been devised as a way to provide a more accurate and 'dynamic' representation of the conformational state of intrinsically disordered proteins. Conformational ensembles function by attempting to represent the various conformations of intrinsically disordered proteins within an ensemble file (the type found at the Protein Ensemble Database).
Protein ensemble files are a representation of a protein that can be considered to have a flexible structure. Creating these files requires determining which of the various theoretically possible protein conformations actually exist. One approach is to apply computational algorithms to the protein data in order to try to determine the most likely set of conformations for an ensemble file.
There are multiple methods for preparing data for the Protein Ensemble Database that fall into two general methodologies – pool and molecular dynamics (MD) approaches (diagrammed in the figure). The pool based approach uses the protein’s amino acid sequence to create a massive pool of random conformations. This pool is then subjected to more computational processing that creates a set of theoretical parameters for each conformation based on the structure. Conformational subsets from this pool whose average theoretical parameters closely match known experimental data for this protein are selected.[17]
The molecular dynamics approach takes multiple random conformations at a time and subjects all of them to experimental data. Here the experimental data is serving as limitations to be placed on the conformations (e.g. known distances between atoms). Only conformations that manage to remain within the limits set by the experimental data are accepted. This approach often applies large amounts of experimental data to the conformations which is a very computationally demanding task.[17]
Protein
Data Type
Protocol
PED ID
References
Sic1/Cdc4 NMR and SAXS Pool-based PED9AAA [18]
p15 PAF NMR and SAXS Pool-based PED6AAA [19]
MKK7 NMR Pool-based PED5AAB [20]
Beta-synuclein NMR MD-based PED1AAD [21]
P27 KID NMR MD-based PED2AAA [22]
(adapted from image in "Computational approaches for inferring the functions of intrinsically disordered proteins"[17])
Protein structure databases[edit]
Protein structure database is a database that is modeled around the various experimentally determined protein structures. The aim of most protein structure databases is to organize and annotate the protein structures, providing the biological community access to the experimental data in a useful way. Data included in protein structure databases often includes 3D coordinates as well as experimental information, such as unit cell dimensions and angles for x-ray crystallography determined structures. Though most instances, in this case either proteins or a specific structure determinations of a protein, also contain sequence information and some databases even provide means for performing sequence based queries, the primary attribute of a structure database is structural information, whereas sequence databases focus on sequence information, and contain no structural information for the majority of entries. Protein structure databases are critical for many efforts in computational biology such as structure based drug design, both in developing the computational methods used and in providing a large experimental dataset used by some methods to provide insights about the function of a protein.[23]
Structure classification[edit]
Protein structures can be grouped based on their similarity or a common evolutionary origin. The Structural Classification of Proteins database[24] and CATH database[25] provide two different structural classifications of proteins. Shared structure between proteins is considered evidence of evolutionary relatedness between proteins and is used group proteins together into protein superfamilies.[26]
Computational prediction of protein structure[edit]
Main article: Protein structure prediction
The generation of a protein sequence is much easier than the determination of a protein structure. However, the structure of a protein gives much more insight in the function of the protein than its sequence. Therefore, a number of methods for the computational prediction of protein structure from its sequence have been developed.[27] Ab initio prediction methods use just the sequence of the protein. Threading and homology modeling methods can build a 3-D model for a protein of unknown structure from experimental structures of evolutionarily-related proteins, called a protein family.
See also[edit]
3did
Biomolecular structure
Gene structure
Nucleic acid structure
Z-matrix conversion from Torsion angles to Cartesian coordinates
References[edit]
Jump up ^ H. Stephen Stoker (1 January 2015). Organic and Biological Chemistry. Cengage Learning. p. 371. ISBN 978-1-305-68645-8.
Jump up ^ Brocchieri L, Karlin S (2005-06-10). "Protein length in eukaryotic and prokaryotic proteomes". Nucleic Acids Research. 33 (10): 3390–3400. doi:10.1093/nar/gki615. PMC 1150220  . PMID 15951512.
Jump up ^ Sanger, F.; Tuppy, H. (1951-09-01). "The amino-acid sequence in the phenylalanyl chain of insulin. I. The identification of lower peptides from partial hydrolysates". The Biochemical Journal. 49 (4): 463–481. doi:10.1042/bj0490463. ISSN 0264-6021. PMC 1197535  . PMID 14886310.
Jump up ^ Sanger, F. (1959-05-15). "Chemistry of Insulin". Science. 129 (3359): 1340–1344. doi:10.1126/science.129.3359.1340. ISSN 0036-8075. PMID 13658959.
Jump up ^ Pauling L, Corey RB, Branson HR (1951). "The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain". Proc Natl Acad Sci USA. 37 (4): 205–211. doi:10.1073/pnas.37.4.205. PMC 1063337  . PMID 14816373.
Jump up ^ Chiang YS, Gelfand TI, Kister AE, Gelfand IM (2007). "New classification of supersecondary structures of sandwich-like proteins uncovers strict patterns of strand assemblage". Proteins. 68 (4): 915–921. doi:10.1002/prot.21473. PMID 17557333.
Jump up ^ Govindarajan S, Recabarren R, Goldstein RA (17 September 1999). "Estimating the total number of protein folds". Proteins. 35 (4): 408–414. doi:10.1002/(SICI)1097-0134(19990601)35:4<408::AID-PROT4>3.0.CO;2-A. PMID 10382668.
Jump up ^ Haynie DT, Xue B (2015). "Superdomain in the protein structure hierarchy: the case of PTP-C2". Protein Science. 24: 874–82. doi:10.1002/pro.2664. PMC 4420535  . PMID 25694109.
Jump up ^ Alberts, Bruce; Alexander Johnson; Julian Lewis; Martin Raff; Keith Roberts; Peter Walters (2002). "The Shape and Structure of Proteins". Molecular Biology of the Cell; Fourth Edition. New York and London: Garland Science. ISBN 0-8153-3218-1.
Jump up ^ Anfinsen, C. (1972). "The formation and stabilization of protein structure". Biochem. J. 128 (4): 737–49. doi:10.1042/bj1280737. PMC 1173893  . PMID 4565129.
Jump up ^ Kendrew, J.C.; Bodo, G.; Dintzis, H. M.; Parrish, R. G.; Wyckoff, H.; Phillips, D.C. (1958). "A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-Ray Analysis". Nature. 181: 662–666. doi:10.1038/181662a0. PMID 13517261.
Jump up ^ Krimm, Samuel; Bandekar, J. (1986). "Vibrational Spectroscopy and Conformation of Peptides, Polypeptides, and Proteins". Advances in Protein Chemistry. Advances in Protein Chemistry. 38 (C): 181–364. doi:10.1016/S0065-3233(08)60528-8. ISBN 9780120342389.
Jump up ^ Lessing, J.; Roy, S.; Reppert, M.; Baer, M.; Marx, D.; Jansen, T.L.C.; Knoester, J.; Tokmakoff, A. (2012). "Identifying Residual Structure in Intrinsically Disordered Systems: A 2D IR Spectroscopic Study of the GVGXPGVG Peptide". J. Am. Chem. Soc. 134: 5032–5035. doi:10.1021/ja2114135. PMID 22356513.
Jump up ^ Jansen, T.L.C.; Knoester, J. (2008). "Two-dimensional infrared population transfer spectroscopy for enhancing structural markers of proteins". Biophys. J. 94: 1818–1825. doi:10.1529/biophysj.107.118851. PMC 2242754  . PMID 17981904.
Jump up ^ Minde DP, Maurice MM, Rüdiger SG (2012). Uversky, Vladimir N, ed. "Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTpp". PLoS ONE. 7 (10): e46147. doi:10.1371/journal.pone.0046147. PMC 3463568  . PMID 23056252. CS1 maint: Multiple names: authors list (link)
Jump up ^ Kumari I, Sandhu P, Ahmed M, Akhter Y. Molecular Dynamics Simulations, Challenges and Opportunities: A Biologist's Prospective. Curr Protein Pept Sci. 2017 Aug 30;18(11):1163-1179. doi: 10.2174/1389203718666170622074741. Link for preprint.
^ Jump up to: a b c d Varadi, Mihaly; Vranken, Wim; Guharoy, Mainak; Tompa, Peter (2015-01-01). "Computational approaches for inferring the functions of intrinsically disordered proteins". Frontiers in Molecular Biosciences. 2: 45. doi:10.3389/fmolb.2015.00045. PMC 4525029  . PMID 26301226.
Jump up ^ Mittag, Tanja; Marsh, Joseph; Grishaev, Alexander; Orlicky, Stephen; Lin, Hong; Sicheri, Frank; Tyers, Mike; Forman-Kay, Julie D. (2010-03-14). "Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase". Structure. 18 (4): 494–506. doi:10.1016/j.str.2010.01.020. ISSN 1878-4186. PMC 2924144  . PMID 20399186.
Jump up ^ De Biasio, Alfredo; Ibáñez de Opakua, Alain; Cordeiro, Tiago N.; Villate, Maider; Merino, Nekane; Sibille, Nathalie; Lelli, Moreno; Diercks, Tammo; Bernadó, Pau (2014-02-18). "p15PAF is an intrinsically disordered protein with nonrandom structural preferences at sites of interaction with other proteins". Biophysical Journal. 106 (4): 865–874. doi:10.1016/j.bpj.2013.12.046. ISSN 1542-0086. PMC 3944474  . PMID 24559989.
Jump up ^ Kragelj, Jaka; Palencia, Andrés; Nanao, Max H.; Maurin, Damien; Bouvignies, Guillaume; Blackledge, Martin; Jensen, Malene Ringkjøbing (2015-03-17). "Structure and dynamics of the MKK7-JNK signaling complex". Proceedings of the National Academy of Sciences of the United States of America. 112 (11): 3409–3414. doi:10.1073/pnas.1419528112. ISSN 1091-6490. PMC 4371970  . PMID 25737554.
Jump up ^ Allison, Jane R.; Rivers, Robert C.; Christodoulou, John C.; Vendruscolo, Michele; Dobson, Christopher M. (2014-11-25). "A relationship between the transient structure in the monomeric state and the aggregation propensities of α-synuclein and β-synuclein". Biochemistry. 53 (46): 7170–7183. doi:10.1021/bi5009326. ISSN 1520-4995. PMC 4245978  . PMID 25389903.
Jump up ^ Sivakolundu, Sivashankar G.; Bashford, Donald; Kriwacki, Richard W. (2005-11-11). "Disordered p27Kip1 exhibits intrinsic structure resembling the Cdk2/cyclin A-bound conformation". Journal of Molecular Biology. 353 (5): 1118–1128. doi:10.1016/j.jmb.2005.08.074. ISSN 0022-2836. PMID 16214166.
Jump up ^ Laskowski, RA. "Protein structure databases". Mol Biotechnol. PMID 21225378.
Jump up ^ Murzin, A. G.; Brenner, S.; Hubbard, T.; Chothia, C. (1995). "SCOP: A structural classification of proteins database for the investigation of sequences and structures" (PDF). Journal of Molecular Biology. 247 (4): 536–540. doi:10.1016/S0022-2836(05)80134-2. PMID 7723011. Archived from the original (PDF) on 26 April 2012.
Jump up ^ Orengo, C. A.; Michie, A. D.; Jones, S.; Jones, D. T.; Swindells, M. B.; Thornton, J. M. (1997). "CATH--a hierarchic classification of protein domain structures". Structure. 5 (8): 1093–1108. doi:10.1016/S0969-2126(97)00260-8. PMID 9309224.
Jump up ^ Holm, L; Rosenström, P (July 2010). "Dali server: conservation mapping in 3D". Nucleic Acids Research. 38 (Web Server issue): W545–9. doi:10.1093/nar/gkq366. PMC 2896194  . PMID 20457744.
Jump up ^ Zhang Y (2008). "Progress and challenges in protein structure prediction". Curr Opin Struct Biol. 18 (3): 342–348. doi:10.1016/j.sbi.2008.02.004. PMC 2680823  . PMID 18436442.
Further reading[edit]
50 Years of Protein Structure Determination Timeline - HTML Version - National Institute of General Medical Sciences at NIH
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