Lawrence J. Parkhurst, Professor
737 Hamilton Hall
Department of Chemistry
University of Nebraska-Lincoln
Lincoln, Nebraska 68588 United States

Current Research:
Our lab is working to understand fundamental processes in the initiation of eukaryotic transcription. Our goal is to understand the structural and energetic features that control the recognition of DNA promoter sequences by TBP (TATA Binding Protein) and the further assembly of the multi-protein transcription initiation complex. We use numerous approaches that include microcalorimetry, steady-state and time-resolved fluorescence and anisotropy in the psec-nsec time regime, stopped-flow rapid reaction kinetics, and molecular dynamic studies of protein-DNA interactions using the university supercomputer.




The TATA-Binding Protein Core Domain in Solution Variably Bends TATA Sequences via a Three-Step Binding Mechanism [tables & figures], Roberto F. Delgadillo, JoDell E. Whittington, Laura K. Parkhurst, and Lawrence J. Parkhurst



TATA-Binding Protein Recognition and Bending of a Consensus Promoter Are Protein Species Dependent, JoDell E. Whittington, Roberto F. Delgadillo, Torrissa J. Attebury, Laura K. Parkhurst, Margaret A. Daugherty, and Lawrence J. Parkhurst



Changes in DNA bending and flexing due to tethered cations detected by fluorescence resonance energy transfer, Sarah L. Williams, Laura K. Parkhurst, and Lawrence J. Parkhurst



Intermediate species possessing bent DNA are present along the pathway to formation of a final TBP-TATA complex, Kay M. Parkhurst, Robyn M. Richards, Michael Brenowitz, and Lawrence J. Parkhurst



A Nanosecond ORD Study of Hemoglobin, Lawrence J. Parkhurst



The binding of ribosomal protein Si to Si-depleted 30S and 70S ribosomes. A fluorescence anisotropy study of the effects of Mg2+, Dixie J. Goss, Lawrence J. Parkhurst, Arkesh M. Mehta, and Albert J. Wahba