W. Stites

发表

Protein−Protein Interactions: Interface Structure, Binding Thermodynamics, and Mutational Analysis

W. Stites, Wesley E. Stites, 1997 .

Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease.

W E Stites, D. Shortle, A. Meeker, 1990, Biochemistry.

In a staphylococcal nuclease mutant the side-chain of a lysine replacing valine 66 is fully buried in the hydrophobic core.

W E Stites, E. Lattman, D. Shortle, 1991, Journal of molecular biology.

Replacement of staphylococcal nuclease hydrophobic core residues with those from thermophilic homologues indicates packing is improved in some thermostable proteins.

W. Stites, Junmei Chen, Junmei Chen, 2004, Journal of molecular biology.

High apparent dielectric constants in the interior of a protein reflect water penetration.

E. Lattman, A. Gittis, B. García-Moreno E., 2000, Biophysical journal.

Experimental measurement of the effective dielectric in the hydrophobic core of a protein.

E. Lattman, A. Gittis, W. Stites, 1997, Biophysical chemistry.

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

Eaton E Lattman, E. Lattman, Kelly K. Lee, 2002, Biophysical journal.

Thermodynamic principles for the engineering of pH-driven conformational switches and acid insensitive proteins.

S. Whitten, W. Stites, A. Robinson, 2011, Biophysical chemistry.

High apparent dielectric constant inside a protein reflects structural reorganization coupled to the ionization of an internal Asp.

M. Stahley, A. Gittis, B. García-Moreno E., 2007, Biophysical journal.

Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability.

W E Stites, W. Stites, J. Sakon, 2000, Journal of molecular biology.

Protein surface hydration mapped by site-specific mutations

A. Zewail, W. Stites, Luyuan Zhang, 2006, Proceedings of the National Academy of Sciences.

Refinement of noncalorimetric determination of the change in heat capacity, ΔCp, of protein unfolding and validation across a wide temperature range

W. Stites, Deepika Talla-Singh, 2008, Proteins.

Mustard gas crosslinking of proteins through preferential alkylation of cysteines

W. Stites, C. Broomfield, M. P. Byrne, 1996, Journal of protein chemistry.

A convenient preparation of derivatives of 3(s)-amino-10(r)-carboxy-1,6-diaza-cyclodeca-2,7-dione the dilactam of L-α, γ-diaminobutyric acid and d-glutamic acid: A β-turn template

W. Stites, D. Kemp, 1988 .

Packing is a key selection factor in the evolution of protein hydrophobic cores.

W E Stites, W. Stites, J Chen, 2001, Biochemistry.

An electrophoretic mobility shift assay for methionine sulfoxide in proteins.

W. Stites, C. Saunders, 2012, Analytical biochemistry.

Proteinminus signProtein Interactions: Interface Structure, Binding Thermodynamics, and Mutational Analysis.

W. Stites, Wesley E. Stites, 1997, Chemical reviews.

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

L. Fink, W. Stites, M. Hauer-Jensen, 2008, Radiation research.

Comparing the effect on protein stability of methionine oxidation versus mutagenesis: steps toward engineering oxidative resistance in proteins.

W. Stites, D. Spencer, Y. H. Kim, 2001, Protein engineering.

Does the oxidation of methionine in thrombomodulin contribute to the hypercoaguable state of smokers and diabetics?

W. Stites, Jeffrey W. Froude, 2007, Medical hypotheses.

Evidence for strained interactions between side-chains and the polypeptide backbone.

D. Shortle, A. Meeker, W. Stites, 1994, Journal of molecular biology.

A First-Order Phase Transition Between a Compact Denatured State and a Random Coil State in Staphylococcal Nuclease

E. Lattman, A. Gittis, W. Stites, 1994 .

Chemically crosslinked protein dimers: Stability and denaturation effects

W. Stites, M. P. Byrne, 1995, Protein science : a publication of the Protein Society.

Energetics of side chain packing in staphylococcal nuclease assessed by systematic double mutant cycles.

W E Stites, W. Stites, J Chen, 2001, Biochemistry.

The M32L substitution of staphylococcal nuclease: disagreement between theoretical prediction and experimental protein stability.

W. Stites, D. Spencer, 1996, Journal of Molecular Biology.

Effects of excluded volume upon protein stability in covalently cross-linked proteins with variable linker lengths.

W. Stites, Y. Kim, 2008, Biochemistry.

Protein-Protein Interactions: Interface Structure, Binding Thermodynamics, and Mutational Analysis

W. Stites, 1997 .

Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease.

J M Schwehm, W E Stites, W. Stites, 1998, Biochemistry.

The pH dependence of staphylococcal nuclease stability is incompatible with a three-state denaturation model.

W. Stites, D. Spencer, G. Bertrand, 2013, Biophysical chemistry.

Compact denatured state of a staphylococcal nuclease mutant by guanidinium as determined by resonance energy transfer.

W. Stites, L. Brand, P. Wu, 1992, Biochemistry.

Oxidation of buried cysteines is slow and an insignificant factor in the structural destabilization of staphylococcal nuclease caused by H2O2 exposure

W. Stites, Y. H. Kim, 2004, Amino Acids.

Energetics of side chain packing in staphylococcal nuclease assessed by exchange of valines, isoleucines, and leucines.

W E Stites, W. Stites, D. Spencer, 2001, Biochemistry.

Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation.

W. Stites, M. P. Byrne, 2007, Biophysical chemistry.

Investigation of biological, chemical and physical processes on and in planetary surfaces by laboratory simulation

S. McKeever, D. Sears, W. Stites, 2002 .

The fluorescence detected guanidine hydrochloride equilibrium denaturation of wild-type staphylococcal nuclease does not fit a three-state unfolding model.

W. Stites, Deepika Talla, 2013, Biochimie.

Changes in stability upon charge reversal and neutralization substitution in staphylococcal nuclease are dominated by favorable electrostatic effects.

B. García-Moreno E., W. Stites, C. A. Fitch, 2003, Biochemistry.

Application of automated methods for determination of protein conformational stability.

J M Schwehm, W E Stites, W. Stites, 1998, Methods in enzymology.

Empirical evaluation of the influence of side chains on the conformational entropy of the polypeptide backbone

W. Stites, J. Pranata, Wesley E. Stites, 1995, Proteins.

The phase transition between a compact denatured state and a random coil state in staphylococcal nuclease is first-order.

E. Lattman, W. Stites, A. Gittis, 1993, Journal of molecular biology.