Assistant Professor in Chemistry & Biochemistry
Main Office: WEL 3.212B
Alternate Office: WEL 3.306
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Research in the Webb group seeks to understand and manipulate the mechanisms of interaction, organization, and self-assembly of biological macromolecules that lead to the complex and emergent properties of living systems. Macromolecular interactions in biological systems are now a major focus of interest. In the post-genomic era, enhanced understanding of the cooperation between biological molecules such as proteins, DNA, RNA, and lipids is necessary to explore the complexity of living cells. Macromolecular interactions lead to emergent properties necessary for life, but can only be studied or understood if the molecular-level details that drive and control those interactions are themselves understood. Furthermore, molecules that promote or disrupt specific macromolecular interactions have vast pharmacological potential. The affinity and specificity of macromolecular interactions are the result of both structural and electrostatic driving forces, but while the field of structural biology has made great advances, much less is understood about electrostatic influences. The Webb group measures electrostatic fields at protein-protein interfaces and seeks to develop computational models that accurately predict these interactions. We do this using vibrational Stark effect (VSE) spectroscopy, in which spectral shifts of a probe oscillator’s energy is related directly to that probe’s local electrostatic environment.
|2013|| Walker, D. M.; Hayes, E. C.; and Webb, L. J., Vibrational Stark Effect Spectroscopy Reveals Complementary Electrostatic Fields Created by Protein-Protein Binding at the Interface of Ras and Ral, Phys. Chem. Chem. Phys. 15:12241-12252.|
|2012||Raigoza, A. F.; Webb, L. J., Molecularly Resolved Images of Peptide-Functionalized Gold Surfaces by Scanning Tunneling Microscopy, J. Am. Chem. Soc. 134:19354-19357.|
|2010||Gallardo, I. F.; Webb, L. J., Tethering Hydrophobic Peptides to Functionalized Self- Assembled Monolayers on Gold Through Two Chemical Linkers Using the Huisgen Cycloaddition, Langmuir 26:18959-18966.|
|2010||Stafford, A. J.; Ensign, D. L.; Webb, L. J., Vibrational Stark Effect Spectroscopy at the Interface of Ras and Rap1A Bound to the Ras Binding Domain of RalGDS Reveals an Electrostatic Mechanism for Protein-Protein Interaction, J. Phys. Chem. B 114:15331-15344.|
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