Principles Governing the Stability and Folding Kinetics of Proteins From Extremophiles
Abstract
The goals attained during this project are: (1) Development of extremely computational methods to study allosteric dynamis in enzymes, molecular motos, and chaperones. (2) Application of these techniques to closed to open transition in the enzyme DHFR. The results were in excellent with experiments. More importantly, our predictions were quantitatively validated in NMR experiments. (2) A fully quantitative simulation of the folding landscape of riboswitches. Remarkably, our predictions were verified in 2011 in single molecule experiments fully three years after the predictions. (3) Identified residues that are responsible for transmitting allosteric signals in motors and chaperones.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 25, 2012
- Accession Number
- ADA567225
Entities
People
- Devarajan Thirumalai
Organizations
- University of Maryland