Unbiased clustering of residues undergoing synchronous motions in proteins using NMR spin relaxation data

Keyphrases

• Synchronous Motion 100%
• Synchronous Dynamics 100%
• NMR Spin Relaxation 100%
• Dynamic Map 100%
• Unbiased Clustering 100%
• Ribonuclease 66%
• Ligand Binding 66%
• Relaxation Dispersion 66%
• Macromolecules 33%
• Biological Function 33%
• Allostery 33%
• Two Dimensional 33%
• Side Chain 33%
• Active Sites 33%
• Catalytic Subunit 33%
• Two-lobe 33%
• Conformational States 33%
• Methyl Groups 33%
• Allosteric Site 33%
• Carr-Purcell-Meiboom-Gill 33%
• Protein Matrix 33%
• Nucleotide Binding 33%
• Biological Macromolecules 33%
• Inherent Flexibility 33%
• Atomic Resolution 33%
• Multi-residue 33%
• Data Dispersion 33%
• Dispersion Measurement 33%
• NMR Relaxation Dispersion 33%
• Dynamic Clustering 33%
• Functional Motion 33%
• Dynamic Cluster 33%
• Bloch-McConnell Equations 33%
• CAMP-dependent Protein Kinase 33%
• Manual Selection 33%
• Unbiased Method 33%
• Pairwise Fitting 33%
• Enzyme-catalyzed 33%
• Backbone Amides 33%
• Dynamic Objects 33%

Chemistry

• NMR Spectroscopy 100%
• Relaxation 100%
• Spin Relaxation 100%
• Macromolecule 100%
• Ligand Binding 100%
• Catalysis 50%
• Nuclear Magnetic Resonance Relaxation 50%
• Methyl Group 50%
• Carboxamide 50%
• Nucleotide 50%
• Allostery 50%
• Kinase A 50%