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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

Thermoswitching of Helical Inversion of Dynamic Polyphenylacetylenes through cis-trans Isomerization of Amide Pendants

TL;DR: The cis-trans isomerization of amides plays a vital role in all kinds of structural changes and biological activities, involving protein folding, protein misfolding, and even protein molecular reco...
Journal ArticleDOI

Resonant Plasmonic Nanoslits Enable in Vitro Observation of Single-Monolayer Collagen-Peptide Dynamics.

TL;DR: Modeling the coupling between the amide I vibrational modes and the plasmonic resonance, this work can extract the conformational state of the collages and thus monitor the folding and unfolding dynamics of even a single monolayer, which leads to new prospects in studies of single layers of proteins and their folding behavior in minute amounts in a living environment.
Book ChapterDOI

The molecular structure of simple substances related to proteins.

TL;DR: This chapter deals with structure of molecules related to protein, which consists of the measurements of the Raman effect, infrared absorption, dielectric constants, electron diffraction, entropies, and specific heats for the determination of stable positions of internal rotation.
DissertationDOI

Ab initio study of alanine-based polypeptide secondary-structure motifs in the gas phase

TL;DR: In this paper, the authors present a first-principle description of the secondary structure of polypeptides in the gas-phase using the OPLS-AA force field.
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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