Deuteration of nonexchangeable protons on proteins affects their thermal stability, side-chain dynamics, and hydrophobicity.

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作者： Parker J,Nichols ^[1] ; Isaac,Falconer ^[2] ; Aaron,Griffin ^[3] ; Colin,Mant ^[2] ; Robert,Hodges ^[1] ; Christopher J,McKnight ^[1] ; Beat,Vögeli ^[3] ; Liliya,Vugmeyster ^[1]

作者单位： Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado, Aurora, Colorado, USA. ^[1] Department of Chemistry, University of Colorado at Denver, Denver, Colorado, USA. ^[2] Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts, USA. ^[3]

关键词 cross-correlation NMR relaxation deuteration protein dynamics reversed-phase HPLC

主题词细菌蛋白质类(Bacterial Proteins);热温度(Hot Temperature);亲水和疏水相互作用(Hydrophobic and Hydrophilic Interactions);核磁共振, 生物分子(Nuclear Magnetic Resonance, Biomolecular);蛋白质折叠(Protein Folding);蛋白质稳定性(Protein Stability);质子(Protons)

DOI 10.1002/pro.3878

PMID 32356390

发布时间 2021-07-02

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