The development of single molecule spectroscopy over the last two decades has made it possible to probe the conformational structure and dynamics of biomolecules with an unprecedented level of detail. Room-temperature Single-Molecule Fluorescence Resonance Energy Transfer (SM-FRET), in particular, provides the ability to probe intra- and inter-molecular distances as a function of time in a direct manner. These experiments also give rise to many new theoretical questions regarding the behavior of single molecules as apposed to averages over large ensembles.Kinetics and thermodynamics of folding of a de novo designed four-helix bundle protein. J. Mol. Biol. ... Hydrophobic interactions in aqueous urea solutions with implications for the mechanism of protein denaturation. J. Am. Chem. Soc ...  Nitin Rathore, Thomas A. Knotts IV, and Juan J. de Pable. Confinement effects on anbsp;...
|Title||:||A computational study of the conformational structure and dynamics of biopolymers in relation to single molecule fluorescence resonance energy transfer measurements|
|Author||:||Jianyuan Shang, University of Michigan|