Rotamer strain as a determinant of protein structural specificity.
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.
Lazar
G A
GA
Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.
Johnson
E C
EC
Desjarlais
J R
JR
Handel
T M
TM
D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D017433:Protein Structure, Secondary; D014452:Ubiquitins / Q000737:chemistry* / Q000235:genetics
D014452:Ubiquitins