Urea-induced unfolding of the .alpha. subunit of tryptophan synthase: One-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration-Reference-Cited by-同舟云学术

Urea-induced unfolding of the .alpha. subunit of tryptophan synthase: One-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration

Published:1993-12-01 Issue:50 Volume:32 Page:13981-13990
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Saab-Rincon Gloria,Froebe Claudia L.,Matthews C. Robert

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00213a031

Reference44 articles.

1. MUTATIONAL EFFECTS ON PROTEIN STABILITY

2. Characterization of an early intermediate in the folding of the .alpha. subunit of tryptophan synthase by hydrogen exchange measurement

3. Effects of the phenylalanine-22 .fwdarw. leucine, glutamic acid-49 .fwdarw. methionine, glycine-234 .fwdarw. aspartic acid and glycine-234 .fwdarw. lysine mutations on the folding and stability of the .alpha. subunit of tryptophan synthase from Escherichia coli

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

5. Solubility of different folding conformers of bovine growth hormone

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