Disulfide crosslinks to probe the structure and flexibility of a designed four‐helix bundle protein
Open Access
- 1 December 1994
- journal article
- research article
- Published by Wiley in Protein Science
- Vol. 3 (12), 2419-2427
- https://doi.org/10.1002/pro.5560031225
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.Keywords
This publication has 40 references indexed in Scilit:
- One-Disulfide Intermediates of Apamin Exhibit Native-Like StructureBiochemistry, 1994
- Metal Ion-Dependent Modulation of the Dynamics of a Designed ProteinScience, 1993
- Stabilities of disulfide bond intermediates in the folding of apaminBiochemistry, 1992
- The molten globule protein conformation probed by disulphide bondsNature, 1991
- Urea dependence of thiol-disulfide equilibria in thioredoxin: confirmation of the linkage relationship and a sensitive assay for structureBiochemistry, 1989
- Intrachain loops in polymers: Effects of excluded volumeThe Journal of Chemical Physics, 1989
- Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1984
- Intermediates in the refolding of reduced ribonuclease AJournal of Molecular Biology, 1979
- Energetics of folding and unfolding of pancreatic trypsin inhibitorJournal of Molecular Biology, 1977
- Conformational restrictions on the pathway of folding and unfolding of the pancreatic trypsin inhibitorJournal of Molecular Biology, 1977