Oxygen Equilibrium Properties of Myoglobin Locked in the Liganded and Unliganded Conformations-Reference-Cited by-同舟云学术

Oxygen Equilibrium Properties of Myoglobin Locked in the Liganded and Unliganded Conformations

Published:2003-03-08 Issue:13 Volume:125 Page:3780-3783
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Shibayama Naoya¹,Saigo Satoshi¹

Affiliation:

1. Contribution from the Department of Physiology, Division of Biophysics, Jichi Medical School, Yakushiji 3311-1, Minamikawachi, Kawachi, Tochigi 329-0498, Japan.

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja029237g

Reference34 articles.

1. A Steric Mechanism for Inhibition of CO Binding to Heme Proteins

2. Protein Conformation Change of Myoglobin upon Ligand Binding Probed by Ultraviolet Resonance Raman Spectroscopy

3. Protein Conformational Relaxation and Ligand Migration in Myoglobin: A Nanosecond to Millisecond Molecular Movie from Time-Resolved Laue X-ray Diffraction

4. Conformational Relaxation and Ligand Binding in Myoglobin

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