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

✍ Scribed by Lynne Regan; Arlene Rockwell; Zelda Wasserman; William Degrado

Book ID: 105356277
Publisher: Cold Spring Harbor Laboratory Press
Year: 1994
Tongue: English
Weight: 980 KB
Volume: 3
Category: Article
ISSN: 0961-8368
DOI: 10.1002/pro.5560031225

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✦ Synopsis

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.

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