scispace - formally typeset
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.

read more

Citations
More filters
Journal ArticleDOI

Interpretation of Infrared Dichroism in Fibrous Proteins —the 2μ Region

TL;DR: In this paper, the assignment of the overtone and combination bands which appear in the infrared spectra of fibrous proteins between 4200 and 5500 cm−1 is discussed on the basis of the normal vibrations of an isolated CO group.
Journal ArticleDOI

Peptide-Coated Silver Nanoparticles: Synthesis, Surface Chemistry, and pH-Triggered, Reversible Assembly into Particle Assemblies

TL;DR: Peptide-controlled silver nanoparticle assembly processes are explored via UV/Vis, X-ray photoelectron, and surface-enhanced Raman spectroscopies as well as through electron microscopy, small angleX-ray scattering and powder X-rays diffraction with Rietveld refinement.
Journal ArticleDOI

Alpha helix capping in synthetic model peptides by reciprocal side chain–main chain interactions: Evidence for an N terminal “capping box”

TL;DR: The side chain–main chain interactions in a varient sequence using 1H NMR are reexamined, and the postulated reciprocal side chain‐backbone bonding between the first Ser and last Glu side chains and their peptide NH partners can be resolved.
Journal ArticleDOI

A prevalent intraresidue hydrogen bond stabilizes proteins.

TL;DR: It is demonstrated that previously unappreciated hydrogen bonds occur within proteins between the amide proton and carbonyl oxygen of the same residue, and inclusion in computational force fields would improve models of protein folding, function, and dysfunction.
Journal ArticleDOI

Palladium-catalyzed Sonogashira coupling of amides: access to ynones via C-N bond cleavage.

TL;DR: The first palladium-catalyzed Sonogashira coupling of amides has been developed, which proceeds via a selective cleavage of the N-acylsaccharin C-N bond, which can be efficiently utilized in the synthesis of a broad array of ynones under low catalyst loading and Cu-free conditions.
References
More filters
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.
Related Papers (5)