Article
A Disordered Loop Mediates Heterogeneous Unfolding of an Ordered Protein by Altering the Native Ensemble.
The journal of physical chemistry letters - 20 Aug 2020
Bhattacharjee Kabita, Gopi Soundhararajan, Naganathan Athi N
Abstract excerpt
The high flexibility of long disordered or partially structured loops in folded proteins allows for entropic stabilization of native ensembles. Destabilization of such loops could alter the native ensemble or promote alternate conformations within the native ensemble if the ordered regions themselves are held together weakly. This is particularly true of downhill folding systems that exhibit weak unfolding...
Topics
- Bacterial Proteins
- Geobacillus stearothermophilus
- Molecular Dynamics Simulation
- Mutation
- Protein Conformation
- Protein Domains
- Protein Unfolding
- Pyruvate Dehydrogenase Complex
- Transition Temperature