The isolated C-terminal (F2) fragment of the Escherichia coli tryptophan synthase .beta.2-subunit folds into a stable, organized nonnative conformation-Reference-Cited by-同舟云学术

The isolated C-terminal (F2) fragment of the Escherichia coli tryptophan synthase .beta.2-subunit folds into a stable, organized nonnative conformation

Published:1991-08-13 Issue:32 Volume:30 Page:8067-8074
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Chaffotte Alain,Guillou Yvonne,Delepierre Muriel,Hinz Hans Jurgen,Goldberg Michel E.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00246a027

Reference41 articles.

1. Identification of three sites of proteolytic cleavage in the hinge region between the two domains of the .beta.2 subunit of tryptophan synthase of Escherichia coli or Salmonella typhimurium

2. Pieces of the folding puzzle

3. A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A.

4. Amide proton exchange used to monitor the formation of a stable α-helix by residues 3 to 13 during folding of ribonuclease S

5. 1H-nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH

Cited by 48 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Pre-Molten, Wet, and Dry Molten Globules en Route to the Functional State of Proteins;International Journal of Molecular Sciences;2023-01-26

2. Protein Dynamics;Encyclopedia of Analytical Chemistry;2011-06-15

3. Iron−Sulfur Cluster Biosynthesis: Characterization of a Molten Globule Domain in Human NFU;Biochemistry;2009-07-17

4. Lack of coupling between secondary structure formation and collapse in a model polypeptide that mimics early folding intermediates, the F2 fragment of the Escherichia coli tryptophan-synthase β chain;Protein Science;2008-12-31

5. Chapter 2 Jacques Monod, Protein Folding and Me;Comprehensive Biochemistry;2008