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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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Fingerprints of inter- and intramolecular hydrogen bonding in saligenin–water clusters revealed by mid- and far-infrared spectroscopy

TL;DR: Infrared (IR) ultraviolet (UV) ion-dip spectroscopy was used to study isolated saligenin-(H2O)n clusters in the far- and mid-IR regions of the spectrum, and harmonic and anharmonic quantum chemical calculations were applied to assign cluster geometries to the measured spectra, and to assign vibrational modes to all spectral features measured for each cluster.
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Effects of Helical Chain Shape on Lamellae-Forming Block Copolymer Self-Assembly

TL;DR: In this paper, the effects of nonideal polymer chain shapes on block copolymer self-assembly were investigated. But the effects on the shape of the polymer chain were not investigated.
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Protein Structure and Folding: A New Start

TL;DR: Characterization of the loop-n-lock units reveals several sequence/structure prototypes, which suggests a new basis for protein classification, and the role of van der Waals contacts in protein stability is better understood.
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Helices in biomolecules

TL;DR: Identical objects, regularly assembled, form a helix, which is the principal motif of nucleic acids, proteins, and viral capsids.
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Integrating single-molecule spectroscopy and simulations for the study of intrinsically disordered proteins.

TL;DR: A comprehensive overview of single-molecule fluorescence spectroscopy and molecular simulations in the context of studying disordered proteins can be found in this paper, where the authors discuss the various means in which simulations can be integrated, and consider a number of studies in which this integration has uncovered biological and biophysical mechanisms.
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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