Structure prediction and modelling.

M B Swindells

doi:10.1016/0958-1669(92)90161-b

Home/Archive/PubMed

PubMed · 1368434

Structure prediction and modelling.

M B Swindells

View original source ↗Export metadata ↓

Abstract

Cracking the second fundamental code of molecular biology (how the tertiary structure of a protein is determined by its amino acid sequence) remains an elusive goal. However, the impetus to establish credible approximations, if not a definitive solution to this relationship, has never been greater. In the past year significant progress has been made through a series of novel approaches. This review describes the most important developments and outlines how they can be usefully employed by those whose specialization lies outside the field.

Explore related subjects

Models, Molecular Protein Conformation Proteins Sequence Alignment Journal Article Review

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

M B Swindells. 1992. Structure prediction and modelling.. https://doi.org/10.1016/0958-1669(92)90161-b

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2003

Experimental and theoretical characterization of H(2)OOO(+).

This report presents the preparation and characterization of H2OOO+, an important intermediate in water-oxygen chemistry. The H2OOO+ cation was produced by co-deposition of H2O/Ar with radio frequency discharged O2/Ar at 4 K and was identified by four fundamental infrared absorptions. Quantum chemical calculations indicate a doublet ground state with a H2O-O2 hemi-bonded Cs structure.

Models, Molecular↗

PubMed2003

The discovery of the alpha-helix and beta-sheet, the principal structural features of proteins.

PNAS papers by Linus Pauling, Robert Corey, and Herman Branson in the spring of 1951 proposed the alpha-helix and the beta-sheet, now known to form the backbones of tens of thousands of proteins. They deduced these fundamental building blocks from properties of small molecules, known both from crystal structures and from Pauling's resonance theory of chemical bonding that predicted planar peptide groups. Earlier attempts by others to build models for protein helices had failed both by including nonplanar peptides and by insisting on helices with an integral number of units per turn. In major respects, the Pauling-Corey-Branson models were astoundingly correct, including bond lengths that were not surpassed in accuracy for >40 years. However, they did not consider the hand of the helix or the possibility of bent sheets. They also proposed structures and functions that have not been found, including the gamma-helix.

Models, Molecular↗

PubMed2003

Automatic model building based on flexible fragment formalism. The case of high-resolution protein structures.

A concept of flexible fragments has been developed for automatic building of crystal structures. Six monopeptides were designed as search fragments in a phased rotation and translation function for protein building. Electron density in crystal and in molecular fragments is expanded in spherical harmonics and normalized spherical Bessel functions. A fast rotation function, which is calculated at each grid point of the asymmetric unit, is used to find the fragment orientation. Position, orientation and internal torsion angles are refined. An algorithm for chain building is simplified using generalized atoms and virtual bonds. The structure is built from molecular structure units rather than from individual atoms. A polyalanine model is built with a high accuracy at resolutions 1.2-2.1 A.

Models, Molecular↗