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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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The fast protein folding problem

TL;DR: During protein folding, many of the events leading to secondary and tertiary structure occur in milliseconds or faster, and modern nuclear magnetic resonance and laser detection techniques are probing these events in great detail.
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Direct detection of transient α-helical states in islet amyloid polypeptide

TL;DR: Rat IAPP is mechanistically informative for fibrillogenesis, as it samples intermediate‐like states but does not progress to form amyloid, and the residues displaying helical propensity are conserved with the human sequence, suggesting a functional role for this conformational bias.
Journal ArticleDOI

A two-step approach to achieve secondary amide transamidation enabled by nickel catalysis

TL;DR: A simple two-step approach is presented that allows for the elusive overall transformation of secondary amide transamidation to take place using non-precious metal catalysis and expands the growing repertoire of new transformations mediated by baseMetal catalysis.
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Super-Resolution in Solution X-Ray Scattering and Its Applications to Structural Systems Biology

TL;DR: A coherent synthesis of SAXS theory and experiment is presented with a focus on analytical tools for accurate, objective, and high-throughput investigations, and hybrid structural methods are discussed, illustrating the role ofSAXS in structure refinement with NMR and ensemble refinement with single-molecule FRET.
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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