Predicted dynamical couplings of protein residues characterize catalysis, transport and allostery.
Alvaro AlfayateCarlos Rodriguez CaceresHelena G. Dos SantosUgo BastollaPublished in: Bioinform. (2019)
Keyphrases
- protein structure
- amino acids
- protein sequences
- solvent accessibility
- experimentally determined
- secondary structure
- amino acid sequences
- contact map
- protein function
- protein folding
- protein structure prediction
- amino acid residues
- protein structure alignment
- protein chains
- amino acid composition
- protein protein
- physicochemical properties
- molecular dynamics simulations
- predicting protein
- molecular biology
- computational biology
- prediction accuracy
- protein structural
- protein tertiary structure
- multiple sequence alignments
- sequence alignment
- molecular dynamics
- computational approaches
- computational methods
- protein interaction data
- subcellular localization
- coarse grained
- protein protein interactions
- mathematical morphology