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Open AccessJournal ArticleDOI

The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain.

Linus Pauling, +2 more
- 01 Apr 1951 - 
- Vol. 37, Iss: 4, pp 205-211
TLDR
This work has used information about interatomic distances, bond angles, and other configurational parameters to construct two reasonable hydrogen-bonded helical configurations for the polypeptide chain; it is likely that these configurations constitute an important part of the structure of both fibrous and globular proteins, as well as of syntheticpolypeptides.
Abstract
During the past fifteen years we have been attacking the problem of the structure of proteins in several ways. One of these ways is the complete and accurate determination of the crystal structure of amino acids, peptides, and other simple substances related to proteins, in order that information about interatomic distances, bond angles, and other configurational parameters might be obtained that would permit the reliable prediction of reasonable configurations for the polypeptide chain. We have now used this information to construct two reasonable hydrogen-bonded helical configurations for the polypeptide chain; we think that it is likely that these configurations constitute an important part of the structure of both fibrous and globular proteins, as well as of synthetic polypeptides. A letter announcing their discovery was published last year [1]. The problem that we have set ourselves is that of finding all hydrogen-bonded structures for a single polypeptide chain, in which the residues are equivalent (except for the differences in the side chain R). An amino acid residue (other than glycine) has no symmetry elements. The general operation of conversion of one residue of a single chain into a second residue equivalent to the first is accordingly a rotation about an axis accompanied by translation along the axis. Hence the only configurations for a chain compatible with our postulate of equivalence of the residues are helical configurations. For rotational angle 180° the helical configurations may degenerate to a simple chain with all of the principal atoms, C, C' (the carbonyl carbon), N, and O, in the same plane.

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Citations
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Predicting the molecular shape of polysaccharides from dynamic interactions with water

TL;DR: A framework is developed to investigate the role of water in the emergence of dynamic structure in polysaccharides, using the important beta(1-->4) linkage as an example.
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Redrawing the Ramachandran plot after inclusion of hydrogen-bonding constraints

TL;DR: It is shown that adding hydrogen-bonding constraints to these steric criteria eliminates another substantial region of φ,ψ-space for a blocked peptide; for conformers within this region, an amide hydrogen is solvent-inaccessible, depriving it of a hydrogen- bonding partner.
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Colloquium: Geometrical approach to protein folding: a tube picture

TL;DR: The authors show here that proteins may be regarded as tubes of nonzero thickness, which allows one to bridge the conventional compact polymer phase with a novel phase employed by Nature to house biomolecular structures.
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A brief history of macromolecular crystallography, illustrated by a family tree and its Nobel fruits

TL;DR: At least 42 scientists who received Nobel Prizes in Physics, Chemistry or Medicine for their contributions that included the use of X‐rays or neutrons and crystallography, including 24 who made seminal discoveries in macromolecular sciences are identified.
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Thermodynamic and Kinetic Stabilities of Complementary Double Helices Utilizing Amidinium–Carboxylate Salt Bridges

TL;DR: The introduction of electron-donating and/or electron-withdrawing substituents at the phenyl groups of the p-diethynylbenzene linkers connecting the amidine and carboxylic acid units tends to stabilize the complementary double helices, especially in polar solvents, such as DMSO, due to the attractive charge-transfer interactions between the aromatic linkers.
References
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Journal ArticleDOI

Two hydrogen-bonded spiral configurations of the polypeptide chain

TL;DR: In this article, two hydrogen-bonded spiral configurations of the polypeptide chain were constructed, with the residues all equivalent, except for variation in the side chain.
Journal ArticleDOI

The Structure of Fibrous Proteins.

Journal ArticleDOI

Nature of the Intramolecular Fold in Alpha-Keratin and Alpha-Myosin

TL;DR: The normal folded configuration a, the extended configuration β, and the reversible intramolecular transformation from a-keratin (or a-myosin) to β-kerATin (or β-myOSin) is the basis of the remarkable long-range elastic properties of this group of protein fibres.
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