Modeling of Ligation-Induced Helix/Loop Displacements in Myoglobin: Toward an Understanding of Hemoglobin Allostery-Reference-Cited by-同舟云学术

Modeling of Ligation-Induced Helix/Loop Displacements in Myoglobin: Toward an Understanding of Hemoglobin Allostery

Published:2006-04-01 Issue:16 Volume:128 Page:5427-5435
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Guallar Victor¹,Jarzecki Andrzej A.¹,Friesner Richard A.¹,Spiro Thomas G.¹

Affiliation:

1. Contribution from the Department of Biochemistry, Washington University School of Medicine, St, Louis, Missouri 63108, Department of Chemistry and Center for Biomolecular Simulations, Columbia University, New York, New York 0027, and Department of Chemistry, Princeton University, Princeton, New Jersey 08544

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja057318h

Reference45 articles.

1. Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism

2. A third quaternary structure of human hemoglobin A at 1.7-A resolution.

3. Quaternary structure of hemoglobin in solution

Cited by 39 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Influence of pump laser fluence on ultrafast myoglobin structural dynamics;Nature;2024-02-14

2. Structural dynamics of proteins explored via time-resolved x-ray liquidography;Chemical Physics Reviews;2022-12

3. Influence of pump laser fluence on ultrafast structural changes in myoglobin;2022-11-22

4. Nonbonded Atomic Contacts Drive Ultrafast Helix Motions in Myoglobin;The Journal of Physical Chemistry B;2020-06-08

5. Predicting Positions of Bridging Water Molecules in Nucleic Acid–Ligand Complexes;Journal of Chemical Information and Modeling;2019-04-18