Can three-dimensional contacts in protein structures be predicted by analysis of correlated mutations?

doi:10.1093/protein/7.3.349

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Article

Can three-dimensional contacts in protein structures be predicted by analysis of correlated mutations?

Protein engineering - 1 Mar 1994

Shindyalov I N, Kolchanov N A, Sander C

Abstract excerpt

A method has been developed to detect pairs of positions with correlated mutations in protein multiple sequence alignments. The method is based on reconstruction of the phylogenetic tree for a set of sequences and statistical analysis of the distribution of mutations in the branches of the tree. The database of homology-derived protein structures (HSSP) is used as the source of multiple sequence alignments for...

Topics

Amino Acid Sequence
Amino Acids
Biological Evolution
Chemical Phenomena
Chemistry, Physical
Cytochrome c Group
DNA-Binding Proteins
Molecular Sequence Data
Molecular Structure
Mutagenesis
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Structure, Secondary

Proteins

Repressor Proteins

Sequence Alignment

Trypsin

Viral Proteins

Viral Regulatory and Accessory Proteins

Source

Open in PubMed

Identifiers

PMID: 8177884
DOI: 10.1093/protein/7.3.349

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8177884-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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