Spectral analysis of a protein conformational switch

S. Rackovsky

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

The existence of conformational switching in proteins, induced by single amino acid mutations, presents an important challenge to our understanding of the physics of protein folding. Sequence-local methods, commonly used to detect structural homology, are incapable of accounting for this phenomenon. We examine a set of proteins, derived from the GA and GB domains of Streptococcus protein G, which are known to show a dramatic conformational change as a result of single-residue replacement. It is shown that these sequences, which are almost identical locally, can have very different global patterns of physical properties. These differences are consistent with the observed complete change in conformation. These results suggest that sequence-local methods for identifying structural homology can be misleading. They point to the importance of global sequence analysis in understanding sequence-structure relationships.

Original languageEnglish
Article number248101
JournalPhysical Review Letters
Volume106
Issue number24
DOIs
StatePublished - 14 Jun 2011

Fingerprint

Dive into the research topics of 'Spectral analysis of a protein conformational switch'. Together they form a unique fingerprint.

Cite this