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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.

SUBMITTER: Yang C 

PROVIDER: S-EPMC6274816 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature

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

Yang Cheolhee C   Choi Minseo M   Kim Jong Goo JG   Kim Hanui H   Muniyappan Srinivasan S   Nozawa Shunsuke S   Adachi Shin-Ichi SI   Henning Robert R   Kosheleva Irina I   Ihee Hyotcherl H  

International journal of molecular sciences 20181118 11


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 <i>Scapharca inaequivalvis</i> 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),  ...[more]

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