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Dynamics fingerprint and inherent asymmetric flexibility of a cold-adapted homodimeric enzyme. A case study of the
Vibrio
alkaline phosphatase
Elena Papaleo
, Giulia Renzetti, Gaetano Invernizzi, Bjarni Asgeirsson
Biomolecular Sciences
15
Citationer (Scopus)
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Keyphrases
Cold-adapted
100%
Alkaline Phosphatase
100%
Homodimeric
100%
Intramolecular Interactions
100%
Vibrio
100%
Intermolecular Interactions
66%
Molecular Dynamics Simulation
33%
Dynamical Patterns
33%
Long-distance Communication
33%
Explicit Solvent
33%
Information Flow
33%
All-atom
33%
Catalytic Residues
33%
Low Temperature
33%
Protein Function
33%
Underlying Network
33%
Dynamic Influence
33%
Conformational Change
33%
Protein Structure
33%
Protein Dynamics
33%
Protein Stability
33%
Homomeric
33%
Biochemistry, Genetics and Molecular Biology
Dynamics
100%
Enzyme
100%
Vibrio
100%
Motion
100%
Alkaline Phosphatase
100%
Protein Structure
33%
Protein Dynamics
33%
Conformational Change
33%
Computer Simulation
33%
Protein Function
33%