Minimization of Cavity Size Ensures Protein Stability and Folding: Structures of Phe46-Replaced Bovine Pancreatic RNase A,-Reference-Cited by-同舟云学术

Minimization of Cavity Size Ensures Protein Stability and Folding: Structures of Phe46-Replaced Bovine Pancreatic RNase A,

Published:2003-08-20 Issue:36 Volume:42 Page:10651-10658
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kadonosono Tetsuya¹,Chatani Eri¹,Hayashi Rikimaru¹,Moriyama Hideaki¹,Ueki Tatzuo¹

Affiliation:

1. Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo, Kyoto 606-8502, Japan, Chemistry and Biotechnology Center, University of Nebraska-Lincoln, Lincoln, Nebraska 68588-0403 USA, and Japan Synchrotron Radiation Research Institute (JASRI), 1-1 Kouto, Mikazuki, Sayo, Hyogo 679-5198, Japan

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi034499w

Reference50 articles.

1. Ribonuclease A

2. Folding pathway of guanidine-denatured disulfide-intact wild-type and mutant bovine pancreatic ribonuclease A

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