Article
Propagated Perturbations from a Peripheral Mutation Show Interactions Supporting WW Domain Thermostability.
Structure (London, England : 1993) - 6 Nov 2018
Zhang Meiling, Case David A, Peng Jeffrey W
Abstract excerpt
Inter-residue interactions stabilize protein folds and facilitate allosteric communication. Predicting which interactions are crucial and understanding why remain challenging. We highlight this through studies of a single peripheral mutation (Q33E) on the surface of the Pin1 WW domain that causes an unexpected loss of thermostability. Nuclear magnetic resonance studies attribute the loss to reorganizations of...
Topics
- Allosteric Regulation
- Humans
- Molecular Dynamics Simulation
- Mutation
- NIMA-Interacting Peptidylprolyl Isomerase
- Protein Binding
- Protein Conformation
- Protein Folding
- Protein Stability
- Thermodynamics
- WW Domains