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

Intramolecularly hydrogen-bonded peptide conformations.

TL;DR: This review focuses both on model peptides and biological activity polypeptide molecules and on intramolecularly hydrogen-bonded peptide structures involving a side-chain group, the N-protecting group, and a beta-amino acid.
Journal ArticleDOI

Protein structure, stability and solubility in water and other solvents.

TL;DR: The authors showed that protein solubility will be markedly lower in polar solvents such as ethanol and that proteins will be essentially insoluble in cyclohexane, and even more stable in a vacuum.
Journal ArticleDOI

DnaK functions as a central hub in the E. coli chaperone network

TL;DR: This work used Escherichia coli as a model to understand the organization of cellular chaperone networks, focusing on the cooperation of the DnaK system with the upstream chaperones Trigger factor (TF) and the downstream GroEL.
Journal ArticleDOI

The Complementary Structure of Deoxyribonucleic Acid

TL;DR: This paper describes a possible structure for the paracrystalline form of the sodium salt of deoxyribonucleic acid that consists of two DNA chains wound helically round a common axis, and held together by hydrogen bonds between specific pairs of bases.
Journal ArticleDOI

Breaking Amides using Nickel Catalysis

TL;DR: Ni catalysis provides exciting new tools to build C-heteroatom and C-C bonds using an unconventional reactant (i.e., the amide), which is ideally suited for use in multi-step synthesis.
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)