Large shifts in pKa values of lysine residues buried inside a protein
Published 2011 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Large shifts in pKa values of lysine residues buried inside a protein
Authors
Keywords
-
Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 108, Issue 13, Pages 5260-5265
Publisher
Proceedings of the National Academy of Sciences
Online
2011-03-10
DOI
10.1073/pnas.1010750108
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Conformational Consequences of Ionization of Lys, Asp, and Glu Buried at Position 66 in Staphylococcal Nuclease
- (2010) Daniel A. Karp et al. BIOCHEMISTRY
- Protein Vivisection Reveals Elusive Intermediates in Folding
- (2010) Zhongzhou Zheng et al. JOURNAL OF MOLECULAR BIOLOGY
- Structural Origins of High Apparent Dielectric Constants Experienced by Ionizable Groups in the Hydrophobic Core of a Protein
- (2010) Michael S. Chimenti et al. JOURNAL OF MOLECULAR BIOLOGY
- Charges in the hydrophobic interior of proteins
- (2010) D. G. Isom et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Exploring challenges in rational enzyme design by simulating the catalysis in artificial kemp eliminase
- (2010) M. P. Frushicheva et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- The pKa Values of Acidic and Basic Residues Buried at the Same Internal Location in a Protein Are Governed by Different Factors
- (2009) Michael J. Harms et al. JOURNAL OF MOLECULAR BIOLOGY
- The origin of the electrostatic perturbation in acetoacetate decarboxylase
- (2009) Meng-Chiao Ho et al. NATURE
- Molecular determinants of the pKavalues of Asp and Glu residues in staphylococcal nuclease
- (2009) Carlos A. Castañeda et al. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
- Crystallographic Study of Hydration of an Internal Cavity in Engineered Proteins with Buried Polar or Ionizable Groups
- (2008) Jamie L. Schlessman et al. BIOPHYSICAL JOURNAL
- pKaof Residue 66 inStaphylococal nuclease. I. Insights from QM/MM Simulations with Conventional Sampling
- (2008) Nilanjan Ghosh et al. JOURNAL OF PHYSICAL CHEMISTRY B
- Influence of nonlinear electrostatics on transfer energies between liquid phases: Charge burial is far less expensive than Born model
- (2008) H. Gong et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Random walk in orthogonal space to achieve efficient free-energy simulation of complex systems
- (2008) L. Zheng et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- 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
Find Funding. Review Successful Grants.
Explore over 25,000 new funding opportunities and over 6,000,000 successful grants.
ExploreCreate your own webinar
Interested in hosting your own webinar? Check the schedule and propose your idea to the Peeref Content Team.
Create Now