pH-Dependent Conformational Changes in Proteins and Their Effect on Experimental pKas: The Case of Nitrophorin 4
Published 2012 View Full Article
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Title
pH-Dependent Conformational Changes in Proteins and Their Effect on Experimental pKas: The Case of Nitrophorin 4
Authors
Keywords
Biochemical simulations, Biophysical simulations, Nitric oxide, Crystal structure, Hydrogen bonding, Molecular dynamics, Simulation and modeling, Thermodynamics
Journal
PLoS Computational Biology
Volume 8, Issue 11, Pages e1002761
Publisher
Public Library of Science (PLoS)
Online
2012-11-02
DOI
10.1371/journal.pcbi.1002761
References
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- Crucial Role of Asp408 in the Proton Translocation Pathway of Multidrug Transporter AcrB: Evidence from Site-Directed Mutagenesis and Carbodiimide Labeling
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- pH-Dependent Mechanism of Nitric Oxide Release in Nitrophorins 2 and 4
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- Effect of Mutation of Carboxyl Side-Chain Amino Acids Near the Heme on the Midpoint Potentials and Ligand Binding Constants of Nitrophorin 2 and Its NO, Histamine, and Imidazole Complexes
- (2009) Robert E. Berry et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Improving the analysis of NMR spectra tracking pH-induced conformational changes: Removing artefacts of the electric field on the NMR chemical shift
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- Backbone Relaxation Coupled to the Ionization of Internal Groups in Proteins: A Self-Guided Langevin Dynamics Study
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- Electrostatic Effects in a Network of Polar and Ionizable Groups in Staphylococcal Nuclease
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- Bond or Cage Effect: How Nitrophorins Transport and Release Nitric Oxide
- (2008) Marcelo A. Martí et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
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