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Protein Sci. 1994 Dec;3(12):2419-27.

Disulfide crosslinks to probe the structure and flexibility of a designed four-helix bundle protein.

Author information

1
Experimental Station, E.I. du Pont de Nemours and Company, Wilmington, Delaware 19880, USA.

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.

PMID:
7756995
PMCID:
PMC2142780
DOI:
10.1002/pro.5560031225
[Indexed for MEDLINE]
Free PMC Article

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