NMR Characterization of Three-Disulfide Variants of Lysozyme, C64A/C80A, C76A/C94A, and C30A/C115AA Marginally Stable State in Folded Proteins-Reference-Cited by-同舟云学术

NMR Characterization of Three-Disulfide Variants of Lysozyme, C64A/C80A, C76A/C94A, and C30A/C115AA Marginally Stable State in Folded Proteins

Published:2004-05-07 Issue:21 Volume:43 Page:6663-6669
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Yokota Atsushi¹,Hirai Kenichi¹,Miyauchi Hiroyo¹,Iimura Satoshi¹,Noda Yasuo¹,Inoue Kyoko¹,Akasaka Kazuyuki¹,Tachibana Hideki¹,Segawa Shin-ichi¹

Affiliation:

1. Japan Science and Technology Corporation, Izumi, Osaka, 594-1144, Japan, Department of Physics, School of Science and Technology, Kwansei Gakuin University, Sanda, 669-1337, Japan, Genome Science Center, RIKEN Yokohama Institute, Yokohama, 230-0045, Japan, Kinki University, School of Biology-Oriented Science and Technology, Wakayama, 649-6493, Japan, and Department of Biology, Faculty of Science, and Graduate School of Science and Technology, Kobe University, Kobe, 657-8501, Japan

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi049967w

Reference24 articles.

1. Efficient in vitro folding of the three-disulfide derivatives of hen lysozyme in the presence of glycerol

2. The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge

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