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.
journal_name
Int J Mol Scijournal_title
International journal of molecular sciencesauthors
Yang C,Choi M,Kim JG,Kim H,Muniyappan S,Nozawa S,Adachi SI,Henning R,Kosheleva I,Ihee Hdoi
10.3390/ijms19113633subject
Has Abstractpub_date
2018-11-18 00:00:00issue
11issn
1422-0067pii
ijms19113633journal_volume
19pub_type
杂志文章,评审abstract：:n/a. ...
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