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Title: Protein Structural Dynamics of Wild-Type and Mutant Homodimeric Hemoglobin Studied by Time-Resolved X-Ray Solution Scattering

Abstract

The quaternary transition between the relaxed (R) and tense (T) states of heme-binding proteins is a textbook example for the allosteric structural transition. Homodimeric hemoglobin (HbI) from Scapharca inaequivalvis is a useful model system for investigating the allosteric behavior because of the relatively simple quaternary structure. To understand the cooperative transition of HbI, wild-type and mutants of HbI have been studied by using time-resolved X-ray solution scattering (TRXSS), which is sensitive to the conformational changes. Herein, we review the structural dynamics of HbI investigated by TRXSS and compare the results of TRXSS with those of other techniques.

Authors:
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Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
DOE - BASIC ENERGY SCIENCESNIH
OSTI Identifier:
1483878
Resource Type:
Journal Article
Journal Name:
International Journal of Molecular Sciences (Online)
Additional Journal Information:
Journal Volume: 19; Journal Issue: 11; Journal ID: ISSN 1422-0067
Publisher:
MDPI
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Yang, Cheolhee, Choi, Minseo, Kim, Jong, Kim, Hanui, Muniyappan, Srinivasan, Nozawa, Shunsuke, Adachi, Shin-ichi, Henning, Robert, Kosheleva, Irina, and Ihee, Hyotcherl. Protein Structural Dynamics of Wild-Type and Mutant Homodimeric Hemoglobin Studied by Time-Resolved X-Ray Solution Scattering. United States: N. p., 2018. Web. doi:10.3390/ijms19113633.
Yang, Cheolhee, Choi, Minseo, Kim, Jong, Kim, Hanui, Muniyappan, Srinivasan, Nozawa, Shunsuke, Adachi, Shin-ichi, Henning, Robert, Kosheleva, Irina, & Ihee, Hyotcherl. Protein Structural Dynamics of Wild-Type and Mutant Homodimeric Hemoglobin Studied by Time-Resolved X-Ray Solution Scattering. United States. doi:10.3390/ijms19113633.
Yang, Cheolhee, Choi, Minseo, Kim, Jong, Kim, Hanui, Muniyappan, Srinivasan, Nozawa, Shunsuke, Adachi, Shin-ichi, Henning, Robert, Kosheleva, Irina, and Ihee, Hyotcherl. Thu . "Protein Structural Dynamics of Wild-Type and Mutant Homodimeric Hemoglobin Studied by Time-Resolved X-Ray Solution Scattering". United States. doi:10.3390/ijms19113633.
@article{osti_1483878,
title = {Protein Structural Dynamics of Wild-Type and Mutant Homodimeric Hemoglobin Studied by Time-Resolved X-Ray Solution Scattering},
author = {Yang, Cheolhee and Choi, Minseo and Kim, Jong and Kim, Hanui and Muniyappan, Srinivasan and Nozawa, Shunsuke and Adachi, Shin-ichi and Henning, Robert and Kosheleva, Irina and Ihee, Hyotcherl},
abstractNote = {The quaternary transition between the relaxed (R) and tense (T) states of heme-binding proteins is a textbook example for the allosteric structural transition. Homodimeric hemoglobin (HbI) from Scapharca inaequivalvis is a useful model system for investigating the allosteric behavior because of the relatively simple quaternary structure. To understand the cooperative transition of HbI, wild-type and mutants of HbI have been studied by using time-resolved X-ray solution scattering (TRXSS), which is sensitive to the conformational changes. Herein, we review the structural dynamics of HbI investigated by TRXSS and compare the results of TRXSS with those of other techniques.},
doi = {10.3390/ijms19113633},
journal = {International Journal of Molecular Sciences (Online)},
issn = {1422-0067},
number = 11,
volume = 19,
place = {United States},
year = {2018},
month = {11}
}