Chain-chain complexation and heme binding in haemoglobin with respect to the hydrophobic core structure

Author:

Ptak Magdalena,Banach Mateusz,Wiśniowski Zdzisław,Konieczny Leszek,Roterman Irena

Abstract

AbstractHeme binding by proteins and protein-protein complexation are the processes strongly related to the biological activity of proteins. The mechanism of these processes has not been still recognised. These phenomena are presented using haemoglobin as the example. Half of the mature haemoglobin (one α-chain and one β-chain) treated as a dissociation step in haemoglobin degradation reveals a specific change in heme binding after dissociation. This phenomenon is the object of analysis that interprets the structure of both complexes (tetramer and dimer) with respect to their hydrophobic core structure. The results suggest the higher stability of the complex in the form of one α-chain and one β-chain with respect to the hydrophobic core.

Publisher

Walter de Gruyter GmbH

Subject

Health Informatics,Biochemistry, Genetics and Molecular Biology (miscellaneous),Medicine (miscellaneous),General Computer Science

Reference64 articles.

1. Heme binding in haemoglobin J Capetown;J Mol Biol,1971

2. The role of residue stability in transient protein-protein interactions involved in enzymatic phosphate hydrolysis. A computational study;Proteins,2006

3. The molecular origin of the control mechanisms in haemoglobin;Bibl Haematol,1968

4. Binding of haem to protein in haemoglobin and myoglobin;Nature,1959

5. Role of alpha-hemoglobin molecular chaperone in the hemoglobin formation and clinical expression of some hemoglobinopathies;Transfus Clin Biol,2015

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3