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Rotamer strain as a determinant of protein structural specificity

Published online by Cambridge University Press:  01 December 1999

GREG A. LAZAR ,
ERIC C. JOHNSON ,
JOHN R. DESJARLAIS  and
TRACY M. HANDEL
GREG A. LAZAR
Affiliation:
Department of Molecular and Cell Biology, Stanley Hall, University of California, Berkeley, California 94720
ERIC C. JOHNSON
Affiliation:
Department of Molecular and Cell Biology, Stanley Hall, University of California, Berkeley, California 94720 Department of Physics, University of California, Berkeley, California 94720
JOHN R. DESJARLAIS
Affiliation:
Department of Chemistry, Chandlee Laboratory, Penn State University, University Park, Pennsylvania 16802
TRACY M. HANDEL
Affiliation:
Department of Molecular and Cell Biology, Stanley Hall, University of California, Berkeley, California 94720
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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.

Keywords

hydrophobic coreNMRpackingprotein designrotamerspecificitystrainubiquitin
Type
Research Article
Information
Protein Science , Volume 8 , Issue 12 , December 1999 , pp. 2598 - 2610
Copyright
© 1999 The Protein Society

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