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NMR Methods for Characterizing the Basic Side Chains of Proteins: Electrostatic Interactions, Hydrogen Bonds, and Conformational Dynamics
Dan Nguyen
, Chuanying Chen
,
B. Montgomery Pettitt
,
Junji Iwahara
Biochemistry & Molecular Biology
Research output
:
Chapter in Book/Report/Conference proceeding
›
Chapter
22
Scopus citations
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Dive into the research topics of 'NMR Methods for Characterizing the Basic Side Chains of Proteins: Electrostatic Interactions, Hydrogen Bonds, and Conformational Dynamics'. Together they form a unique fingerprint.
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Keyphrases
NMR Techniques
100%
Side Chain
100%
Electrostatic Interaction
100%
Conformational Dynamics
100%
Basic Side Chains
100%
Hydrogen Bond Dynamics
100%
Protein Electrostatics
100%
Lysine
75%
Protein Dynamics
50%
Arginine
50%
Ion Pairs
25%
Molecular Dynamics
25%
Hydrogen Bonds (H-bonds)
25%
NMR Spectroscopy
25%
Protein Function
25%
Positively Charged
25%
Molecular Dynamics Simulation
25%
Dynamic Study
25%
NMR Data
25%
Aromatics
25%
Highly Dynamic
25%
NMR Studies
25%
Dynamic Nature
25%
Protein Backbone
25%
Protein Side Chains
25%
Dynamic NMR
25%
Cationic Groups
25%
Biochemistry, Genetics and Molecular Biology
Dynamics
100%
Hydrogen Bond
100%
Static Electricity
100%
Lysine
75%
Motion
50%
Protein Dynamics
50%
Arginine
50%
Protein Function
25%
Nuclear Magnetic Resonance Spectroscopy
25%