Circular dichroism spectroscopy of bovine pancreatic trypsin inhibitor and five altered conformational states. Relationship of conformation and the refolding pathway of the trypsin inhibitor-Reference-Cited by-同舟云学术

Circular dichroism spectroscopy of bovine pancreatic trypsin inhibitor and five altered conformational states. Relationship of conformation and the refolding pathway of the trypsin inhibitor

Published:1981-09-29 Issue:20 Volume:20 Page:5744-5754
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/bi00523a017

Reference65 articles.

1. The Disulfide Linkages in Kallikrein Inactivator of Bovine Lung

2. On the Optical Activity of Ionized Tyrosyl Residues in Ovine Lutropin

3. Optical activity of disulfide bonds in proteins: 2. Studies on human choriomammotropin and bovine pituitary somatotropin

4. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues

5. Unfolding and refolding occur much faster for a proline-free proteins than for most proline-containing proteins.

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