Richard J. Wittebort, PhD

Research Program

Structural Biology

Research Interests

(Chemistry): fibrous peptides-solid state NMR

The research in my laboratory is concerned with experimental studies of molecular dynamics and peptide conformation in the solid state using NMR techniques coupled with computational work. Our current interests are in the conformations of fibrous proteins such as collagen and elastin, and their interactions with water. The new 18.8 T NMR instrument will be exceptionally valuable for making measurements on these systems, which cannot be studied by single crystal diffraction or solution state NMR techniques.

Education

Education/Training

B.S., Ohio State University, Ohio, Biochemistry, 1972

Ph.D., Indiana University, Bloomington, Indiana, Chemistry, 1978

Post-Doc, Massachusetts Institute of Technology, Massachusetts, Chemical Physics, 1978-1980

Research and Professional Experience

1981-1985         
Assistant Professor, Department of Chemistry, University of Louisville, Louisville, Kentucky

1985-1988         
Associate Professor, Department of Chemistry, University of Louisville

1988-present     
Professor, Department of Chemistry, University of Louisville

2001-present     
Senior Scientist, James Graham Brown Cancer Center, University of Louisville

Selected Awards and Professional Honors

1970-1971
N.S.F. Undergraduate Research, Ohio State University

1972
Indiana University Foundation Fellow

1973-1977
Predoctoral Trainee, National Institutes of Health, Indiana University

1978-1980
Postdoctoral Fellow, National Institutes of Health, Massachusetts Institute of Technology

2002-present
Advisory Panel, National High Field Magnet Lab, Florida State University

Publications

Mack JW, Usha MG, Long J, Griffin RG, Wittebort RJ. Backbone motions in a crystalline protein from field dependent 2H NMR relaxation and lineshape analysis.  Biopolymers 53:9-17, 2000

Pometun MS, Gundusharma UM, Richardson JF, Wittebort RJ. Solid state NMR and calorimetry of structural waters in helical peptides.  J Am Chem Soc 124:2345-51, 2002

Shekar SC, Ramamoorthy A, Wittebort RJ. Determination of the chemical shielding tensor orientation from two or one of the three conventional rotations of a single crystal.  J Magn Reson 155:257-62, 2002

Chekmenev EY, Xu RZ, Mashuta MS, Wittebort RJ. Clycyl Ca chemical shielding in tripeptides: measurement by solid-state NMR and correlation with X-ray structure and theory.  J Am Chem Soc 124:11894-9, 2002

Zhang Q, Chekmenev EY, Wittebort RJ. 17O quadrupole coupling and chemical shielding tensors in an H-bonded carboxyl group: oxalic acid.  J Am Chem Soc 125:9140-6, 2003

Cheruzel LE, Pometun MS, Cecil MR, Wittebort RJ, Buchanan RM. Structures and solid state dynamics of one-dimensional water chains stabilized by imidazole channels.  Angewandte Chem Int Ed 42:5452-5, 2003

Zhang Q, Chekmenev EY, Wittebort RJ. 17O quadrupole coupling and chemical shielding tensors in an H-bonded carboxyl group: alpha-oxalic acid.  J Am Chem Soc 125:9140-6, 2003

Fan TW, Lane AN, Chekmenev E, Wittebort RJ, Higashi RM. Synthesis and physicochemical properties of peptides in soil humic substances.  J Pept Res 63:253-64, 2004

Chekmenev EY, Zhang Q, Waddell KW, Mashuta MS, Wittebort RJ. 15N chemical shielding in glycyl tripeptides: measurement by solid-state NMR and correlation with X-ray structure.  J Am Chem Soc 126:379-84, 2004

Pometun MS, Chekmenev EY, Wittebort RJ. Quantitative observation of backbone disorder in native elastin.  J Biol Chem 279:7982-7, 2004

Waddell KW, Chekmenev EY, Wittebort RJ. Single-crystal studies of peptide prolyl and glycyl 15N shielding tensors.  J Am Chem Soc 127:9030-5, 2005

Phone: Coming soon.

 

 

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