Circular dichroism spectroscopy of the intermediates that precede the rate-limiting step of the refolding pathway of bovine pancreatic trypsin inhibitor. Relationship of conformation and the refolding pathway-Reference-Cited by-同舟云学术

Circular dichroism spectroscopy of the intermediates that precede the rate-limiting step of the refolding pathway of bovine pancreatic trypsin inhibitor. Relationship of conformation and the refolding pathway

Published:1983-05-10 Issue:10 Volume:22 Page:2433-2440
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kosen Phyllis Anne,Creighton Thomas E.,Blout Elkan R.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00279a020

Reference30 articles.

1. Determination of the helix and β form of proteins in aqueous solution by circular dichroism

2. The single-disulphide intermediates in the refolding of reduced pancreatic trypsin inhibitor

3. The two-disulphide intermediates and the folding pathway of reduced pancreatic trypsin inhibitor

4. Interactions between cysteine residues as probes of protein conformation: The bisulphide bond between Cys-14 and Cys-38 of the pancreatic trypsin inhibitor

5. Conformational restrictions on the pathway of folding and unfolding of the pancreatic trypsin inhibitor

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