Prediction of local structural stabilities of proteins from their amino acid sequences.
Hydrogen exchange experiments provide detailed information about the local stability and the solvent accessibility of different regions of the structures of folded proteins, protein complexes, and amyloid fibrils. We introduce an approach to predict protection factors from hydrogen exchange in proteins based on the knowledge of their amino acid sequences without the inclusion of any additional structural information. These results suggest that the propensity of different regions of the structures of globular proteins to undergo local unfolding events can be predicted from their amino acid sequences with an accuracy of 80% or better.
Tartaglia
Gian Gaetano
GG
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.
Cavalli
Andrea
A
Vendruscolo
Michele
M
D000595:Amino Acid Sequence; D000818:Animals; D019295:Computational Biology / Q000379:methods*; D006801:Humans; D006859:Hydrogen / Q000737:chemistry; D008956:Models, Chemical; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
D011506:Proteins; D006859:Hydrogen