Lawrence Parkhurst

Lawrence Parkhurst.

Emeritus Professor,
Hewett University Professor
Chemistry

737 Hamilton Hall
Lincoln, NE 68588
(402) 472-3316
lparkhurst1@unl.edu
Faculty Profile

Parkhurst Research Group
Education
  • Ph.D., Yale University
  • M.S., Yale University
  • B.S., Yale University

Research Interests
  • Biomolecular sciences
  • Laser chemistry
Selected Publications
  • A small molecule directly inhibits the p53 transactivation domain from binding to replication protein A By: Glanzer, Jason G.; Carnes, Katie A.; Soto, Patricia; et al. NUCLEIC ACIDS RESEARCH Volume: 41 Issue: 3 Pages: 2047-2059 Published: FEB 2013.
  • TATA-Binding Protein Recognition and Bending of a Consensus Promoter Are Protein Species Dependent, Whittington, J. E., Delgadillo, R. F., Attebury, T., Parkhurst, L. K., Daugherty, M. A. and Parkhurst, L. J., Biochemistry (2008), published on the Web 06/14/2008.
  • Changes in DNA bending and flexing due to tethered cations detected by fluorescence resonance energy transfer Williams, Sarah L.; Parkhurst, Laura K.; Parkhurst, Lawrence J.. Department of Chemistry, University of Nebraska-Lincoln, Lincoln, NE, USA. Nucleic Acids Research (2006), 34(3), 1028-1035.
  • Native Human TATA-binding Protein Simultaneously Binds and Bends Promoter DNA without a Slow Isomerization Step or TFIIB Requirement K. M. Masters, K. M. Parkhurst, M. A. Daugherty, L. J. Parkhurst, Journal of Biological Chemistry 2003, 278, 31685-31690.
  • Comparison of TATA-binding protein recognition of a variant and consensus DNA promoters R. M. Powell, K. M. Parkhurst, L. J. Parkhurst, Journal of Biological Chemistry 2002, 277, 7776-7784.
  • Time-resolved fluorescence resonance energy transfer studies of DNA bending in double-stranded oligonucleotides and in DNA-protein complexes L. J. Parkhurst, K. M. Parkhurst, R. Powell, J. Wu, S. Williams, Biopolymers 2002, 67, 180-200.
  • DNA bends in TATA-binding protein.TATA complexes in solution are DNA sequence-dependent J. Wu, K. M. Parkhurst, R. M. Powell, M. Brenowitz, L. J. Parkhurst, Journal of Biological Chemistry 2001, 276, 14614-14622.
  • DNA sequence-dependent differences in TATA-binding protein-induced DNA bending in solution are highly sensitive to osmolytes J. Wu, K. M. Parkhurst, R. M. Powell, L. J. Parkhurst, Journal of Biological Chemistry 2001, 276, 14623-14627.
  • Marked stepwise differences within a common kinetic mechanism characterize TATA-binding protein interactions with two consensus promoters R. M. Powell, K. M. Parkhurst, M. Brenowitz, L. J. Parkhurst, Journal of Biological Chemistry 2001, 276, 29782-29791.