Understanding mutations and protein stability through tripeptides.


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.

Cite this paper

@article{Anishetty2006UnderstandingMA, title={Understanding mutations and protein stability through tripeptides.}, author={Sharmila Anishetty and Ramesh Anishetty and Gautam Pennathur}, journal={FEBS letters}, year={2006}, volume={580 8}, pages={2071-80} }