ABSTRACT: The protein−water interface is a critical determinant of protein structure and function, yet the precise nature of dynamics in this complex system remains elusive. Tryptophan fluorescence has become the probe of choice for such dynamics on the picosecond time scale (especially via fluorescence “upconversion”). In the absence of ultrafast (“quasi-static”) quenching from nearby groups, the TDFSS (time-dependent fluorescence Stokes shift) for exposed Trp directly reports on dipolar relaxation near the interface (both water and polypeptide). The small protein GB1 contains a single Trp (W43) of this type, and its structure is refractory to pH above 3. Thus, it can be used to examine the dependence of dipolar relaxation upon charge reco...
Fully atomistic molecular dynamics simulations have been carried out to investigate the correlation ...
The unique features of a macromolecule and water as a solvent make the issue of solvation unconventi...
Biological water at the interface of proteins is critical to their equilibrium structures and enzyme...
The protein–water interface is a critical determinant of protein structure and function, yet the pre...
Author Institution: Departments of Physics, Chemistry, and Biochemistry, The Ohio State University, ...
Time-resolved fluorescence spectroscopy is used increasingly to probe molecular motions at the aqueo...
The bioprotective nature of disaccharides is hypothesized to derive from the modification of the hyd...
Author Institution: Department of Physics, The Ohio State University, Columbus, Oh, 43210Although tr...
Intramolecular dynamics in Na,K-ATPase molecules have been studied by ultraviolet fluorescence spect...
Author Institution: Department of Physics, The Ohio State University, Columbus, OH 43210; Department...
AbstractAlthough dielectric relaxation can significantly affect the intrinsic fluorescence propertie...
Time dependent fluorescence Stokes (emission wavelength) shifts (TDFSS) from tryptophan (Trp) follow...
Water has a profound effect on the dynamics of biomolecules and governs many biological processes, l...
Water motion probed by intrinsic tryptophan shows the significant slowdown around protein surfaces, ...
The unique features of a macromolecule and water as a solvent make the issue of solvation unconventi...
Fully atomistic molecular dynamics simulations have been carried out to investigate the correlation ...
The unique features of a macromolecule and water as a solvent make the issue of solvation unconventi...
Biological water at the interface of proteins is critical to their equilibrium structures and enzyme...
The protein–water interface is a critical determinant of protein structure and function, yet the pre...
Author Institution: Departments of Physics, Chemistry, and Biochemistry, The Ohio State University, ...
Time-resolved fluorescence spectroscopy is used increasingly to probe molecular motions at the aqueo...
The bioprotective nature of disaccharides is hypothesized to derive from the modification of the hyd...
Author Institution: Department of Physics, The Ohio State University, Columbus, Oh, 43210Although tr...
Intramolecular dynamics in Na,K-ATPase molecules have been studied by ultraviolet fluorescence spect...
Author Institution: Department of Physics, The Ohio State University, Columbus, OH 43210; Department...
AbstractAlthough dielectric relaxation can significantly affect the intrinsic fluorescence propertie...
Time dependent fluorescence Stokes (emission wavelength) shifts (TDFSS) from tryptophan (Trp) follow...
Water has a profound effect on the dynamics of biomolecules and governs many biological processes, l...
Water motion probed by intrinsic tryptophan shows the significant slowdown around protein surfaces, ...
The unique features of a macromolecule and water as a solvent make the issue of solvation unconventi...
Fully atomistic molecular dynamics simulations have been carried out to investigate the correlation ...
The unique features of a macromolecule and water as a solvent make the issue of solvation unconventi...
Biological water at the interface of proteins is critical to their equilibrium structures and enzyme...