BROWSE

Related Scientist

Researcher

양철희
나노물질 및 화학반응 연구단
more info

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

Cited 0 time in webofscience Cited 0 time in scopus
13 Viewed 2 Downloaded
Title
Protein Structural Dynamics of Wild-Type and Mutant Homodimeric Hemoglobin Studied by Time-Resolved X-Ray Solution Scattering
Author(s)
Cheolhee Yang; Minseo Choi; Jong Goo Kim; Hanui Kim; Srinivasan Muniyappan; Shunsuke Nozawa; Shin-ichi Adachi; Robert Henning; Irina Kosheleva; Hyotcherl Ihee
Publication Date
2018-11
Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, v.19, no.11, pp.3633 -
Publisher
MDPI AG
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. © 2018 by the authors.
URI
https://pr.ibs.re.kr/handle/8788114/5331
ISSN
1422-0067
Appears in Collections:
Center for Nanomaterials and Chemical Reactions(나노물질 및 화학반응 연구단) > Journal Papers (저널논문)
Files in This Item:
Int. J. Mol. Sci. 2018, 19, 3633.pdfDownload

qrcode

  • facebook

    twitter

  • Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.
해당 아이템을 이메일로 공유하기 원하시면 인증을 거치시기 바랍니다.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse