Ion Mobility Mass Spectrometry Analysis of Oxygen Affinity-Associated Structural Changes in Hemoglobin-Reference-Cited by-同舟云学术

Ion Mobility Mass Spectrometry Analysis of Oxygen Affinity-Associated Structural Changes in Hemoglobin

Published:2021-08-31 Issue:10 Volume:32 Page:2528-2535
ISSN:1044-0305
Container-title:Journal of the American Society for Mass Spectrometry
language:en
Short-container-title:J. Am. Soc. Mass Spectrom.

Author:

Heo Chae Eun¹²,Kim Minji¹²,Son Myung Kook¹²,Hyun Da Gyeong¹²,Heo Sung Woo³,Kim Hugh I.¹²^ORCID

Affiliation:

1. Department of Chemistry, Korea University, Seoul 02841, Republic of Korea

2. Center for Proteogenome Research, Korea University, Seoul 02841, Republic of Korea

3. Inorganic Metrology Group, Division of Chemical and Biological Metrology, Korea Research Institute of Standards and Science (KRISS), Daejeon 34113, Republic of Korea

Funder

National Research Foundation of Korea

Korea Research Institute of Standards and Science

Korea Basic Science Institute

Korea Institute of Science and Technology Information

Publisher

American Chemical Society (ACS)

Subject

Spectroscopy,Structural Biology

Link

https://pubs.acs.org/doi/pdf/10.1021/jasms.1c00161

Reference50 articles.

1. Regulation of Oxygen Affinity of Hemoglobin: Influence of Structure of the Globin on the Heme Iron

2. Structure and function of haemoglobin

3. Protein dynamics explain the allosteric behaviors of hemoglobin

4. Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*

5. Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery

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