Predicting isomorphic residue replacements for protein design

E Tüdös; M Cserzö; I Simon

doi:10.1111/j.1399-3011.1990.tb00973.x

Predicting isomorphic residue replacements for protein design

Int J Pept Protein Res. 1990 Sep;36(3):236-9. doi: 10.1111/j.1399-3011.1990.tb00973.x.

Authors

E Tüdös¹, M Cserzö, I Simon

Affiliation

¹ Institute of Enzymology, Hungarian Academy of Sciences, Budapest.

PMID: 2279846
DOI: 10.1111/j.1399-3011.1990.tb00973.x

Abstract

The replaceability of amino acids as reflected in their neighbourhood selectivity is analyzed in this paper. Neighbourhood selectivity was found to be more characteristic of the individual amino acids than the other commonly used parameters. The residue replacement rank obtained was compared with other proposed ranks and was tested on naturally accepted point mutations in homologous proteins.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Amino Acids / chemistry
Drug Design*
Molecular Sequence Data
Molecular Structure
Mutagenesis, Site-Directed
Mutation
Protein Conformation
Proteins / chemistry*
Proteins / genetics

Substances

Amino Acids
Proteins