Understanding mutations and protein stability through tripeptides.

Sharmila Anishetty; Ramesh Anishetty; Gautam Pennathur

doi:10.1016/j.febslet.2006.02.079

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Understanding mutations and protein stability through tripeptides.

Sharmila Anishetty·Ramesh Anishetty·Gautam Pennathur

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Abstract

A novel methodology to predict the local conformational changes in a protein as a consequence of missense mutations is proposed. A pentapeptide at the locus of mutation plays the dominant role and it is analyzed in terms of tripeptides. A measure for spatial and temporal fluctuations in a pentapeptide is devised and validated. The method does not involve any prior knowledge of structural templates from sequence homology studies. Structural deformations can be predicted with about 70-80% reliability in any protein. Disease causing mutations and benign mutations have been addressed. In particular, p53, retinoblastoma protein and lipoprotein lipase are studied in detail.

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Amino Acid Motifs Cross-Sectional Studies Crystallography, X-Ray Databases, Protein Humans Mutation, Missense Peptides Protein Conformation Thermodynamics Tumor Suppressor Protein p53 Journal Article Research Support, Non-U.S. Gov't

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Sharmila Anishetty, Ramesh Anishetty, Gautam Pennathur. 2006-03-10. Understanding mutations and protein stability through tripeptides.. https://doi.org/10.1016/j.febslet.2006.02.079

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