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- W2111909811 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 non-homologous proteins are structurally superimposed. As a baseline for statistical assessment we use the conservatism expected based on the solvent accessibility. The analysis is based on a new concept of conservatism-of-conservatism. This approach allows us to identify the structural features that are stabilized in all proteins having a given fold, despite the fact that actual interactions that provide such stabilization may vary from protein to protein. Comparison with experimental data on thermodynamics, folding kinetics and function of the proteins reveals that such universally conserved clusters correspond to either: (i) super-sites (common location of active site in proteins having common tertiary structures but not function) or (ii) folding nuclei whose stability is an important determinant of folding rate, or both (in the case of Rossman fold). The analysis also helps to clarify the relation between folding and function that is apparent for some folds." @default.
- W2111909811 created "2016-06-24" @default.
- W2111909811 creator A5017406892 @default.
- W2111909811 creator A5082765817 @default.
- W2111909811 date "1999-09-01" @default.
- W2111909811 modified "2023-09-24" @default.
- W2111909811 title "Universally conserved positions in protein folds: reading evolutionary signals about stability, folding kinetics and function" @default.
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- W2111909811 doi "https://doi.org/10.1006/jmbi.1999.2911" @default.
- W2111909811 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10438614" @default.
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