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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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Journal ArticleDOI

Dissecting the energetics of protein alpha-helix C-cap termination through chemical protein synthesis.

TL;DR: Analysis of the thermodynamic data revealed that the preference for glycine at the C′ position of a helix is predominantly a conformational effect, and the contributions of conformational strain and backbone solvation can thus be separated.
Book ChapterDOI

CD Spectroscopy and the Helix-Coil Transition in Peptides and Polypeptides

TL;DR: The alpha helix could be identified in the diffraction patterns from crystals of the globular proteins myoglobin and hemoglobin, as well as in the classical “α” patterns from fibrous proteins like keratin and synthetic polypeptides, poly(γ-l-glutamate) being the first to show the α pattern.
Journal ArticleDOI

Structural change of keratin protein in human hair by permanent waving treatment

TL;DR: In this paper, the damage to human hair caused by permanent waving treatment was examined from the viewpoint of structure with several spectroscopic methods, 13C CP/MAS n.m., wide angle X-ray diffraction (WAXD), FTi.r. and Raman methods.
Journal ArticleDOI

Conformational aspects of polypeptides. XXV. Solvent and temperature effects on the conformations of copolymers of benzyl and methyl L-aspartate with nitrobenzyl L-aspartate.

TL;DR: For the first time, the circular dichroism spectra in which the n‐π* peptide band of a left‐handed helical conformation is almost completely evident are reported.
Journal ArticleDOI

Minimal peptide motif for non-covalent peptide-heparin hydrogels

TL;DR: In this article, minimal peptide motifs whose conjugates with polyethylene glycol interact with heparin to form non-covalent hydrogels were designed and screened.
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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