publication . Other literature type . Article . 1999

Universally conserved positions in protein folds: reading evolutionary signals about stability, folding kinetics and function.

Leonid A. Mirny; Eugene I. Shakhnovich;
  • Published: 01 Sep 1999
  • Publisher: Elsevier BV
Abstract
Here, we provide an analysis of molecular evolution of five of the most populated protein folds: immunoglobulin fold, oligonucleotide-binding fold, Rossman fold, alpha/beta plait, and TIM barrels. In order to distinguish between ‘‘historic’’, functional and structural reasons for amino acid conservations, we consider proteins that acquire the same fold and have no evident sequence homology. For each fold we identify positions that are conserved within each individual family and coincide when nonhomologous proteins are structurally superimposed. As a baseline for statistical assessment we use the conservatism expected based on the solvent accessibility. The analy...
Subjects
free text keywords: Molecular Biology, Phi value analysis, TIM barrel, Molecular evolution, Protein folding, Protein Data Bank (RCSB PDB), Biochemistry, Rossmann fold, Threading (protein sequence), Immunoglobulin domain, Biology
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publication . Other literature type . Article . 1999

Universally conserved positions in protein folds: reading evolutionary signals about stability, folding kinetics and function.

Leonid A. Mirny; Eugene I. Shakhnovich;