Christopher C. Ross, Stewart L. MacLeod, Jason R. Plaxco, Jeffrey W. Froude, Louis M. Fink, Junru Wang, ...
Ross, C. C., MacLeod, S. L., Plaxco, J. R., Froude, J. W., Fink, L. M., Wang, J., Stites, W. E. and Hauer-Jensen, M. Inactivation of Thrombomodulin by Ionizing Radiation in a Cell-Free System:...
Protein surface hydration mapped by site-specific mutations (2006)
Qiu, Weihong, Kao, Ya-Ting, Zhang, Luyuan, Yang, Yi, Wang, Lijuan, Stites, Wesley E., ...
Water motion at protein surfaces is fundamental to protein structure, stability, dynamics, and function. By using intrinsic tryptophans as local optical probes, and with femtosecond resolution, it is...
Fitch, Carolyn A, Karp, Daniel A, Lee, Kelly K, Stites, Wesley E, Lattman, Eaton E
Lys-66 and Glu-66, buried in the hydrophobic interior of staphylococcal nuclease by mutagenesis, titrate with pK(a) values of 5.7 and 8.8, respectively (Dwyer et al., Biophys. J. 79:1610-1620;...
Fitch, Carolyn A, Karp, Daniel A, Lee, Kelly K, Stites, Wesley E, Lattman, Eaton E
Lys-66 and Glu-66, buried in the hydrophobic interior of staphylococcal nuclease by mutagenesis, titrate with pK(a) values of 5.7 and 8.8, respectively (Dwyer et al., Biophys. J. 79:1610-1620;...
Protein surface hydration mapped by site-specific mutations
Qiu, Weihong, Kao, Ya-Ting, Zhang, Luyuan, Yang, Yi, Wang, Lijuan, Stites, Wesley E., ...
Water motion at protein surfaces is fundamental to protein structure, stability, dynamics, and function. By using intrinsic tryptophans as local optical probes, and with femtosecond resolution, it is...
Karp, Daniel A., Gittis, Apostolos G., Stahley, Mary R., Fitch, Carolyn A., Stites, Wesley E.
The dielectric properties of proteins are poorly understood and difficult to describe quantitatively. This limits the accuracy of methods for structure-based calculation of electrostatic energies and...