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Protein structure
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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 Protein structure and stability
3 Domains, motifs, and folds in protein structure
3.1 Structural domain
3.2 Structural and sequence motif
3.3 Supersecondary structure
3.4 Protein fold
3.5 Superdomain
4 Protein folding
5 Protein structure determination
5.1 Protein Sequence Analysis: Ensembles
6 Protein structure databases
7 Structure classification
8 Computational prediction of protein structure
9 See also
10 References
11 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. A well studied protein trimer is Bacteriorhodopsin. These trimers form nice hexagonal lattice[7]. 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.
Protein structure and stability[edit]
Protein stability is depended upon a few factors such as 1) Non-covalent electrostatic interactions 2) Hydrophobic interactions These interaction energies are from the order of 20-40 kJ/mol. Proteins are very sensitive to changing temperatures and a change in temperature may result in unfolding or denaturation. Protein denaturation may result in loss of function, and loss of native state.
X-ray crystallography and calorimetry indicates that there is no general mechanism that describes the effect of temperature change on the functions and structure of proteins. This is due to the fact that proteins do not represent a uniform class of chemical entities from an energetic point of view. The structure and stability of an individual protein depends on the ratio of its polar and non-polar residues. They contribute to the conformational and the net enthalpies of local and non-local interactions.
Taking the weak intermolecular interactions responsible for structural integrity into consideration, it is hard to predict the effects of temperature because there are too many unknown factors contributing to the hypothetical free energy balance and its temperature dependence. Internal salt linkages produce thermal stability, and whether cold temperature results in the destabilization of these linkages is unknown.
In principle, the free energy of stabilization of soluble globular proteins does not exceed 50-100 kJ/mol. The stabilization is based on the equivalent of few hydrogen bonds, ion pairs, or hydrophobic interactions, even though numerous intramolecular interactions results in stabilization. Taking into consideration the large number of hydrogen bonds that take place for the stabilization of secondary structures, and the stabilization of the inner core through hydrophobic interactions, the free energy of stabilization emerges as small difference between large numbers. Therefore, the structure of a native protein is not optimized for the maximum stability.[8]
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.[9] 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.[10] 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.[11] 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).[12]
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.[13] 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.[14] 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.[15][16] 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.[17] Once a protein's structure has been experimentally determined, further detailed studies can be done computationally, using molecular dynamic simulations of that structure.[18]
Protein Sequence Analysis: Ensembles[edit]
Schematic view of the two main ensemble modeling approaches.[19]
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.[19]
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.[19]
Protein
Data Type
Protocol
PED ID
References
Sic1/Cdc4 NMR and SAXS Pool-based PED9AAA [20]
p15 PAF NMR and SAXS Pool-based PED6AAA [21]
MKK7 NMR Pool-based PED5AAB [22]
Beta-synuclein NMR MD-based PED1AAD [23]
P27 KID NMR MD-based PED2AAA [24]
(adapted from image in "Computational approaches for inferring the functions of intrinsically disordered proteins"[19])
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.[25]
Structure classification[edit]
Protein structures can be grouped based on their similarity or a common evolutionary origin. The Structural Classification of Proteins database[26] and CATH database[27] 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.[28]
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.[29] 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]
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Further reading[edit]
50 Years of Protein Structure Determination Timeline - HTML Version - National Institute of General Medical Sciences at NIH
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text:
Military leadership in the American Civil War
From Wikipedia, the free encyclopedia
Jump to: navigation, search
Military leadership in the American Civil War was influenced by professional military education and the hard-earned pragmatism of command experience. While not all leaders had formal military training, the United States Military Academy at West Point, New York and the United States Naval Academy at Annapolis created dedicated cadres of professional officers whose understanding of military science had profound effect on the conduct of the American Civil War and whose lasting legacy helped forge the traditions of the modern U.S. officer corps of all service branches.
Contents
[hide]
1 The Union
1.1 Civilian military leaders
1.2 Regular Army officers
1.3 Militia and political leaders appointed to Union military leadership
1.4 Native American and international officers in Union Army
1.5 Union naval leaders
2 The Confederacy
2.1 Civilian military leaders
2.2 Former Regular Army officers
2.3 Militia and political leaders appointed to Confederate military leadership
2.4 Native American and international officers in Confederate army
2.5 Confederate naval leaders
3 See also
4 Notes
5 References
6 Further reading
The Union[edit]
Ulysses S. Grant
William T. Sherman
George G. Meade
Admiral David Farragut
Civilian military leaders[edit]
President Abraham Lincoln was Commander-in-Chief of the Union armed forces throughout the conflict; after his April 14, 1865 assassination, Vice President Andrew Johnson became the nation's chief executive.[1] Lincoln's first Secretary of War was Simon Cameron; Edwin M. Stanton was confirmed to replace Cameron in January 1862. Thomas A. Scott was Assistant Secretary of War. Gideon Welles was Secretary of the Navy, aided by Assistant Secretary of the Navy Gustavus Fox.[2]
Regular Army officers[edit]
When the war began, the American standing army or "Regular army" consisted of only 1080 commissioned officers and 15,000 enlisted men.[3] Although 142 regular officers became Union generals during the war, most remained "frozen" in their regular units. That stated, most of the major Union wartime commanders had significant previous regular army experience.[4] Over the course of the war, the Commanding General of the United States Army was, in order of service, Winfield Scott, George B. McClellan, Henry Halleck, and finally, Ulysses S. Grant.

Robert Anderson
Don Carlos Buell
John Buford
Ambrose Burnside
Edward Canby
Philip St. George Cooke
Jacob Dolson Cox
Thomas Turpin Crittenden
Thomas Leonidas Crittenden
Samuel Curtis
Abner Doubleday
James A. Garfield
Quincy Adams Gillmore
Ulysses S. Grant
Henry Wager Halleck
Winfield Scott Hancock
Joseph Hooker
Andrew A. Humphreys
Henry Jackson Hunt
George B. McClellan
Irvin McDowell
James B. McPherson
Joseph K. Mansfield
George Meade
Montgomery C. Meigs
Dixon S. Miles
Edward Ord
John Pope
John F. Reynolds
William Rosecrans
John Schofield
Winfield Scott
John Sedgwick
Philip Sheridan
William T. Sherman
Andrew Jackson Smith
William Farrar Smith
George Stoneman
George Henry Thomas
Alfred Thomas Archimedes Torbert
Gouverneur K. Warren
John E. Wool
Militia and political leaders appointed to Union military leadership[edit]
Under the United States Constitution, each state recruited, trained, equipped, and maintained local militia; regimental officers were appointed and promoted by state governors. After states answered Lincoln's April 15, 1861, ninety-day call for 75,000 volunteer soldiers, most Union states' regiments and batteries became known as "Volunteers" to distinguish between state and regular army units. Union brigade-level officers (generals) could receive two different types of Federal commissions: U.S. Army or U.S. Volunteers (ex: Major General, U.S.A. as opposed to Major General, U.S.V.). While most Civil War generals held volunteer or brevet rank, many generals held both types of commission; regular rank was considered superior.[5]
Edward D. Baker
Nathaniel Prentice Banks
Francis Preston Blair, Jr.
Benjamin Franklin Butler
Joshua Lawrence Chamberlain
John Adams Dix
John C. Frémont
John Alexander McClernand
Daniel Sickles
Native American and international officers in Union Army[edit]
Reflecting the multi-national makeup of the soldiers engaged, some Union military leaders derived from nations other than the United States.
Philippe, Comte de Paris
Michael Corcoran
Włodzimierz Krzyżanowski
Thomas Francis Meagher
Ely Parker
Albin F. Schoepf
Carl Schurz
Franz Sigel
Régis de Trobriand
Ivan Turchaninov
Union naval leaders[edit]
The rapid rise of the United States Navy during the Civil War contributed enormously to the North's ability to effectively blockade ports and Confederate shipping from quite early in the conflict. Handicapped by an aging 90 ship fleet, and despite significant manpower losses to the Confederate Navy after secession, a massive ship construction campaign embracing technological innovations from civil engineer James Buchanan Eads and naval engineers like Benjamin F. Isherwood and John Ericsson, along with four years' daily experience with modern naval conflict put the U. S. Navy onto a path which has led to today's world naval dominance.[6]
John A. Dahlgren
Charles Henry Davis
Samuel Francis du Pont
David Farragut
Andrew Hull Foote
Samuel Phillips Lee
David Dixon Porter
John Ancrum Winslow
John Lorimer Worden
The Confederacy[edit]
Jefferson Davis
Robert E. Lee
T.J. "Stonewall" Jackson
James Longstreet
Joseph E. Johnston
James Waddell
Civilian military leaders[edit]
Jefferson Davis was named provisional president on February 9, 1861, and assumed similar commander-in-chief responsibilities as would Lincoln; on November 6, 1861 Davis was elected President of the Confederate States of America under the Confederate Constitution. Alexander H. Stephens was appointed as Vice President of the Confederate States of America on February 18, 1861, and later assumed identical vice presidential responsibilities as Hannibal Hamlin did. Several men served the Confederacy as Secretary of War, including Leroy Pope Walker, Judah P. Benjamin, George W. Randolph, James Seddon, and John C. Breckinridge. Stephen Mallory was Confederate Secretary of the Navy throughout the conflict.[7]
Former Regular Army officers[edit]
In the wake of secession, many regular officers felt they could not betray loyalty to their home state, as a result some 313 of those officers resigned their commission and in many cases took up arms for the Confederate Army. Himself a graduate of West Point and a former regular officer, Confederate President Jefferson Davis highly prized these valuable recruits to the cause and saw that former regular officers were given positions of authority and responsibility.[8]
Richard H. Anderson
P.G.T. Beauregard
Milledge Luke Bonham
Braxton Bragg
Simon Bolivar Buckner, Sr.
George B. Crittenden
Samuel Cooper
Jubal Anderson Early
Richard S. Ewell
Franklin Gardner
Robert S. Garnett
Josiah Gorgas
William Joseph Hardee
Ambrose Powell Hill
Daniel Harvey Hill
John Bell Hood
Thomas J. "Stonewall" Jackson
Albert Sidney Johnston
Joseph E. Johnston
Robert E. Lee
Stephen D. Lee
Mansfield Lovell
James Longstreet
John B. Magruder
Humphrey Marshall
Dabney Herndon Maury
John Hunt Morgan
John C. Pemberton
George Pickett
Edmund Kirby Smith
Gustavus Woodson Smith
J.E.B. Stuart
William B. Taliaferro
Earl Van Dorn
Joseph Wheeler
Henry A. Wise
Militia and political leaders appointed to Confederate military leadership[edit]
The land of Davy Crockett and Andrew Jackson, the state military tradition was especially strong in southern states, some of which were until recently frontier areas. Several significant Confederate military leaders emerged from state unit commands.
John C. Breckinridge
Benjamin F. Cheatham
Nathan Bedford Forrest
Wade Hampton
James L. Kemper
Ben McCulloch
Leonidas Polk
Sterling Price
Richard Taylor
Native American and international officers in Confederate army[edit]
While no foreign power sent troops or commanders directly to assist the Confederate States, some leaders derived from countries other than the United States.
Patrick Cleburne
Stand Watie
Camille Armand Jules Marie, Prince de Polignac
Raleigh E. Colston
Collett Leventhorpe
George St. Leger Grenfell
Confederate naval leaders[edit]
The Confederate Navy possessed no extensive shipbuilding facilities; instead, it relied on refitting captured ships or purchased warships from Great Britain. The South had abundant navigable inland waterways, but after the Union built a vast fleet of gunboats, they soon dominated the Mississippi, Tennessee, Cumberland, Red and other rivers, rendering those waterways almost useless to the Confederacy. Confederates did seize several Union Navy vessels in harbor after secession and converted a few into ironclads, like the CSS Virginia. Blockade runners were built and operated by British naval interests, although by late in the war the C.S. Navy operated some. A few new vessels were built or purchased in Britain, notably the CSS Shenandoah and the CSS Alabama. These warships acted as raiders, wreaking havoc with commercial shipping. Aggrieved by these losses, in 1871 the U.S. government was awarded damages from Great Britain in the Alabama Claims.[6]
John Mercer Brooke
Isaac Newton Brown
Franklin Buchanan
James Dunwoody Bulloch
Catesby ap Roger Jones
Matthew Fontaine Maury
Raphael Semmes
Josiah Tattnall
James Iredell Waddell
See also[edit]
Civil War Generals
History of Confederate States Army Generals
Confederate States Armed Forces
Union Army
Union Navy
Notes[edit]
Jump up ^ Boatner 483, 437
Jump up ^ Boatner 858, 728, 303
Jump up ^ Boatner 673, 858
Jump up ^ Boatner 673
Jump up ^ Boatner 858, 328
^ Jump up to: a b Boatner 582
Jump up ^ Boatner 225, 170
Jump up ^ Boatner 495, 225, 674
References[edit]
Boatner, Mark Mayo, III. The Civil War Dictionary. New York: McKay, 1959; revised 1988. ISBN 0-8129-1726-X.
Eicher, John and David Eicher, Civil War High Commands, Stanford University Press, 2001, ISBN 0-8047-3641-3
Warner, Ezra J., Generals in Blue: Lives of the Union Commanders, Louisiana State University Press, 1964, ISBN 0-8071-0822-7
Warner, Ezra J., Generals in Gray: Lives of the Confederate Commanders, Louisiana State University Press, 1959, ISBN 0-8071-0823-5
Waugh, John C., The Class of 1846, From West Point to Appomattox: Stonewall Jackson, George McClellan and their Brothers, New York: Warner, 1994. ISBN 0-446-51594-9
Further reading[edit]
American National Biography (20 vol. 2000; online and paper copies at academic libraries) short biographies by specialists
Current, Richard N., et al. eds. Encyclopedia of the Confederacy (1993) (4 Volume set; also 1 vol abridged version) (ISBN 0-13-275991-8)
Dictionary of American Biography 30 vol, 1934–1990; short biographies by specialists
Faust, Patricia L. (ed.) Historical Times Illustrated Encyclopedia of the Civil War (1986) (ISBN 0-06-181261-7) 2000 short entries
Heidler, David Stephen. Encyclopedia of the American Civil War: A Political, Social, and Military History (2002), 1600 entries in 2700 pages in 5 vol or 1-vol editions
Woodworth, Steven E. ed. American Civil War: A Handbook of Literature and Research (1996) (ISBN 0-313-29019-9), 750 pages of historiography and bibliography
[hide]
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American Civil War
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Origins
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Antebellum era
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Compromise of 1850
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Missouri Compromise
Popular sovereignty
Secession
States' rights
President Lincoln's 75,000 volunteers
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Foreign Assistance Act
From Wikipedia, the free encyclopedia
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Foreign Assistance Act (1961)
Other short titles
Act for International Development of 1961
Foreign Aid Authorization Act of 1961
Long title
An Act to promote the foreign policy, security, and general welfare of the United States by assisting peoples of the world in their efforts toward economic and social development and internal and external security, and for other purposes.
Nicknames
Foreign Assistance Act of 1961
Enacted by
the 87th United States Congress
Effective
September 4, 1961
Citations
Public law
87-195
Statutes at Large
75 Stat. 424-2
Codification
Titles amended
22 U.S.C.: Foreign Relations and Intercourse
U.S.C. sections created
22 U.S.C. ch. 32 § 2151
Legislative history
Introduced in the Senate as S. 1983 by James W. Fulbright (D-AR) on May 26, 1961
Committee consideration by Senate Foreign Relations, House Foreign Affairs
Passed the Senate on August 18, 1961 (66–24)
Passed the House on August 18, 1961 (287-140, in lieu of H.R. 8400)
Reported by the joint conference committee on August 31, 1961; agreed to by the Senate on August 31, 1961 (69–24) and by the House on August 31, 1961 (260–132)
Signed into law by President John F. Kennedy on September 4, 1961
Major amendments
Foreign Assistance Act of 1974
The Foreign Assistance Act (Pub.L. 87–195, 75 Stat. 424-2, enacted September 4, 1961, 22 U.S.C. § 2151 et seq.) is a United States Act of Congress. The Act reorganized the structure of existing U.S. foreign assistance programs, separated military from non-military aid, and created a new agency, the United States Agency for International Development (USAID) to administer those non-military, economic assistance programs. On November 3, 1961, President John F. Kennedy signed the Act and issued Executive Order 10973, detailing the reorganization.[1]
The agency unified already existing U.S. aid efforts, combining the economic and technical assistance operations of the International Cooperation Administration, the loan activities of the Development Loan Fund, the local currency functions of the Export-Import Bank, and the agricultural surplus distribution activities of the Food for Peace program of the Department of Agriculture.
The Act states that no assistance will be provided to a government which "engages in a consistent pattern of gross violations of internationally recognized human rights, including torture or cruel, inhuman, or degrading treatment or punishment, prolonged detention without charges, causing the disappearance of persons by the abduction and clandestine detention of those persons, or other flagrant denial of the right to life, liberty, and the security of person, unless such assistance will directly benefit the needy people in such country."[2]
The Act also states that no assistance will be provided to any Communist country, however the President may waive this prohibition if he determines that such assistance is vital to the national security of the United States, that the country is not controlled by the international Communist conspiracy, and that the assistance will promote the country's independence from international Communism, the President may also remove a country from the application of this provision for a certain time which the President determines, in order to remove a country from the application of this provision, the President must determine and report to Congress that such action is important to the national security of the United States.
The Act was amended in 2004 specific to the treatment of orphans and other vulnerable children. This amendment allows the president to provide aid to the peoples of other countries to look after children in cases of HIV/AIDS and to set up schools and other programs for the advancement of child treatment.[3][4]
Contents
[hide]
1 Amendments to 1961 Act
2 See also
3 Notes
4 External links
Amendments to 1961 Act[edit]
Chronological timeline of amendments and revisions to the Foreign Assistance Act of 1961.
Date of Enactment
Public Law Number
U.S. Statute Citation
U.S. Legislative Bill
U.S. Presidential Administration
August 1, 1962 Pub.L. 87–565 76 Stat. 255 S. 2996 John F. Kennedy
December 16, 1963 Pub.L. 88–205 77 Stat. 379 H.R. 7885 Lyndon B. Johnson
October 7, 1964 Pub.L. 88–633 78 Stat. 1009 H.R. 11380 Lyndon B. Johnson
September 6, 1965 Pub.L. 89–171 79 Stat. 653 H.R. 7750 Lyndon B. Johnson
March 18, 1966 Pub.L. 89–371 80 Stat. 74 H.R. 12169 Lyndon B. Johnson
September 19, 1966 Pub.L. 89–583 80 Stat. 795-3 H.R. 15750 Lyndon B. Johnson
November 14, 1967 Pub.L. 90–137 81 Stat. 445 S. 1872 Lyndon B. Johnson
October 8, 1968 Pub.L. 90–554 82 Stat. 960 H.R. 15263 Lyndon B. Johnson
January 5, 1971 Pub.L. 91–652 84 Stat. 1942 H.R. 19911 Richard M. Nixon
December 30, 1974 Pub.L. 93–559 88 Stat. 1795 S. 3394 Gerald R. Ford
June 30, 1976 Pub.L. 94–329 90 Stat. 729 H.R. 13680 Gerald R. Ford
September 8, 2017 Pub.L. 115–56 131 Stat. 1129 H.R. 601 Donald Trump
See also[edit]
Alliance for Progress
Arms Export Control Act
Foreign Military Sales Act of 1968
Iran-Contra
Office of Public Safety (OPS)
U.S. Foreign Policy
War on Drugs
War on Terror
Notes[edit]
Jump up ^ Executive Order 10973, 3 November 1961, Administration of Foreign Assistance and Related Functions
Jump up ^ "22 U.S. Code § 8422 - Authorization of assistance". Legal Information Institute. Retrieved 12 March 2015.
Jump up ^ H.R. 1298 at Congress.gov
Jump up ^ "United States Leadership Against HIV/AIDS, Tuberculosis, and Malaria Act of 2003 ~ P.L. 108-25" (PDF). 117 Stat. 711 ~ House Bill 1298. U.S. Government Printing Office. May 27, 2003.
External links[edit]
The Foreign Assistance Act of 1961, as amended
Information from USAID
Foreign Operations Appropriations: General Provisions
FAA-related documents and publications available through USAID's Development Experience Clearinghouse
Peters,Gerhard; Woolley, John T. "John F. Kennedy: "Statement by the President Upon Signing the Foreign Assistance Act.," September 4, 1961". The American Presidency Project. University of California - Santa Barbara. Retrieved September 22, 2013.
"Bill signing - S. 2996 Public Law 87-565, Foreign Assistance Act, 10:29AM". John F. Kennedy Presidential Library and Museum.
Retrieved from "https://en.wikipedia.org/w/index.php?title=Foreign_Assistance_Act&oldid=841194591"
Categories:
1961 in American law
United States foreign relations legislation
United States Agency for International Development
1961 in international relations
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