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Disulfide crosslinks to probe the structure and flexibility of a designed four-helix bundle protein
L Regan1, A Rockwell, Z Wasserman
1Experimental Station, E.I. du Pont de Nemours and Company, Wilmington, Delaware 19880, USA.
Protein Science : a Publication of the Protein Society
|December 1, 1994
Abstract:
The introduction of disulfide crosslinks is a generally useful method by which to identify regions of a protein that are close together in space. Here we describe the use of disulfide crosslinks to investigate the structure and flexibility of a family of designed 4-helix bundle proteins. The results of these analyses lend support to our working model of the proteins' structure and suggest that the proteins have limited main-chain flexibility.