| Literature DB >> 10631975 |
G A Lazar1, E C Johnson, J R Desjarlais, T M Handel.
Abstract
We present direct evidence for a change in protein structural specificity due to hydrophobic core packing. High resolution structural analysis of a designed core variant of ubiquitin reveals that the protein is in slow exchange between two conformations. Examination of side-chain rotamers indicates that this dynamic response and the lower stability of the protein are coupled to greater strain and mobility in the core. The results suggest that manipulating the level of side-chain strain may be one way of fine tuning the stability and specificity of proteins.Mesh:
Substances:
Year: 1999 PMID: 10631975 PMCID: PMC2144231 DOI: 10.1110/ps.8.12.2598
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725