Solution Structure of Horse Heart Ferricytochrome c and Detection of Redox-Related Structural Changes by High-Resolution 1H NMR,-Reference-Cited by-同舟云学术

Solution Structure of Horse Heart Ferricytochrome c and Detection of Redox-Related Structural Changes by High-Resolution 1H NMR,

Published:1996-01-01 Issue:38 Volume:35 Page:12275-12286
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Qi Phoebe Xiurong¹,Beckman Robert A.¹,Wand A. Joshua¹

Affiliation:

1. Departments of Biological Sciences, Biophysical Sciences, and Chemistry and Center for Structural Biology, 816 Natural Sciences Complex, State University of New York at Buffalo, Buffalo, New York 14260-3000

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi961042w

Reference56 articles.

1. Hydrogen bonding in globular proteins

2. Statistical strategy for stereospecific hydrogen NMR assignments: Validation procedures for the floating prochirality method

3. Oxidation state-dependent conformational changes in cytochrome c

4. The protein data bank: A computer-based archival file for macromolecular structures

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