Abstract：
:We describe the physicochemical characterization of various circular and linear forms of the approximately 60 residue N-terminal Src homology 3 (SH3) domain from the murine c-Crk adapter protein. Structural, dynamic, thermodynamic, kinetic and biochemical studies reveal that backbone circularization does not prevent the adoption of the natural folded structure in any of the circular proteins. Both the folding and unfolding rate of the protein increased slightly upon circularization. Circularization did not lead to a significant thermodynamic stabilization of the full-length protein, suggesting that destabilizing enthalpic effects (e.g. strain) negate the expected favorable entropic contribution to overall stability. In contrast, we find circularization results in a dramatic stabilization of a truncated version of the SH3 domain lacking a key glutamate residue. The ability to rescue the destabilized mutant indicates that circularization may be a useful tool in protein engineering programs geared towards generating minimized proteins.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Camarero JA,Fushman D,Sato S,Giriat I,Cowburn D,Raleigh DP,Muir TWdoi
10.1006/jmbi.2001.4631keywords:
subject
Has Abstractpub_date
2001-05-18 00:00:00pages
1045-62issue
5eissn
0022-2836issn
1089-8638pii
S0022-2836(01)94631-5journal_volume
308pub_type
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