标题
Large shifts in pKa values of lysine residues buried inside a protein
作者
关键词
-
出版物
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 108, Issue 13, Pages 5260-5265
出版商
Proceedings of the National Academy of Sciences
发表日期
2011-03-10
DOI
10.1073/pnas.1010750108
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。- Conformational Consequences of Ionization of Lys, Asp, and Glu Buried at Position 66 in Staphylococcal Nuclease
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- Influence of nonlinear electrostatics on transfer energies between liquid phases: Charge burial is far less expensive than Born model
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- High tolerance for ionizable residues in the hydrophobic interior of proteins
- (2008) D. G. Isom et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- A buried lysine that titrates with a normal pKa: Role of conformational flexibility at the protein-water interface as a determinant of pKavalues
- (2008) Michael J. Harms et al. PROTEIN SCIENCE
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