Wesley E. Stites

Publication List Details

Period

2006 - 2008

Number

6

Co-Authors

Inactivation of Thrombomodulin by Ionizing Radiation in a Cell-Free System: Possible Implications for Radiation Responses in Vascular Endothelium (2008)

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...

Experimental pK(a) values of buried residues: analysis with continuum methods and role of water penetration.

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;...

Experimental pK(a) values of buried residues: analysis with continuum methods and role of water penetration.

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...

High Apparent Dielectric Constant Inside a Protein Reflects Structural Reorganization Coupled to the Ionization of an Internal Asp

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...