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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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Formation of one-dimensional helical columns and excimerlike excited states by racemic quinoxaline-fused [7]carbohelicenes in the crystal.

TL;DR: The time-resolved fluorescence spectra of single crystals clearly showed an excimerlike delocalized excited state owing to the short distance between neighboring [7]carbohelicene units, and the absolute fluorescence quantum yields of HeQu derivatives are about four times larger than that of Heli.
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A systematic study of minima in alanine dipeptide

TL;DR: To locate all energy minima, starting from geometries from MD simulations, 250,000 geometry optimizations were performed at the level of RHF/6‐31G*, followed by re‐optimizations of the located 827 minima at thelevel of MP2/6–311++G**, yielding 30 unique minima; most of which were not previously reported in literature.
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William Thomas Astbury. 1898-1961

TL;DR: With the death of William Thomas Astbury on 4 June 1961, there passed one of the most characteristic figures of what may be called the heroic age of crystal structure analysis—the first generation to follow the Braggs—but he was more than this.
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Atomic force microscopy and force spectroscopy on the assessment of protein folding and functionality.

TL;DR: The potential of AFM-based force spectroscopy in the study of protein folding is intended to be demonstrated, especially since this technique is able to circumvent some of the difficulties typically encountered in classical thermal/chemical denaturation studies.
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Facile synthesis of stereoregular helical poly(phenyl isocyanide)s and poly(phenyl isocyanide)-block-poly(L-lactic acid) copolymers using alkylethynylpalladium(II) complexes as initiators

TL;DR: In this paper, a family of air-stable alkylethynyl Pd(II) complexes was unexpectedly found to promote the living polymerization of phenyl isocyanide, affording poly(phenyl iso-yanide)s with controlled molecular weights, narrow molecular weight distributions and high stereoregularity.
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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