High Hydrostatic Pressure Can Reverse Aggregation of Protein Folding Intermediates and Facilitate Acquisition of Native Structure
Author:
Affiliation:
1. Department of Biochemistry, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, Texas 78284
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi9730137
Reference20 articles.
1. Stable intermediates can be trapped during the reversible refolding of urea-denatured rhodanese.
2. The molten globule protein conformation probed by disulphide bonds
3. In vitro folding of inclusion body proteins
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