标题
Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1
作者
关键词
NOESY Spectrum, Dime Interface, Residual Dipolar Coupling, Sedimentation Velocity Experiment, Mammalian sHSPs
出版物
JOURNAL OF BIOMOLECULAR NMR
Volume 63, Issue 2, Pages 223-228
出版商
Springer Nature
发表日期
2015-08-04
DOI
10.1007/s10858-015-9973-0
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Effect of disulfide crosslinking on thermal transitions and chaperone-like activity of human small heat shock protein HspB1
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- Independent evolution of the core domain and its flanking sequences in small heat shock proteins
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- Crystal Structures of α-Crystallin Domain Dimers of αB-Crystallin and Hsp20
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- αB-Crystallin: A Hybrid Solid-State/Solution-State NMR Investigation Reveals Structural Aspects of the Heterogeneous Oligomer
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