DISULFIDE CROSS-LINKS TO PROBE THE STRUCTURE AND FLEXIBILITY OF A DESIGNED 4-HELIX BUNDLE PROTEIN

Authors
REGAN L ROCKWELL A WASSERMAN Z DEGRADO W
Citation
L. Regan et al., DISULFIDE CROSS-LINKS TO PROBE THE STRUCTURE AND FLEXIBILITY OF A DESIGNED 4-HELIX BUNDLE PROTEIN, Protein science, 3(12), 1994, pp. 2419-2427
Citations number
38
Categorie Soggetti
Biology
Journal title
Protein science → ACNP
ISSN journal
09618368
Volume
3
Issue
12
Year of publication
1994
Pages
2419 - 2427
Database
ISI
SICI code
0961-8368(1994)3:12<2419:DCTPTS>2.0.ZU;2-J
Abstract
The introduction of disulfide crosslinks is a generally useful method by which to identify regions of a protein that are close together in s pace, Here we describe the use of disulfide crosslinks to investigate the structure and flexibility of a family of designed 4-helix bundle p roteins. The results of these analyses lend support to our working mod el of the proteins' structure and suggest that the proteins have limit ed main-chain flexibility.