Lauren Webb

lwebb@cm.utexas.edu

Assistant Professor

Research Group

Webb Research Group

Education

Chemistry A.B., Bowdoin College, 2000
Ph.D, California Institute of Technology, 2005

NIH Postdoctoral Fellow, Stanford University, 2005-2008

Awards

Iota Sigma Pi Agnes Fay Morgan Research Award, 2011

College of Natural Sciences Teaching Excellence Award, 2009
Burroughs Wellcome Fund Career Award at the Scientific Interface, 2007-present
National Institutes of Health National Research Service Award, 2006-2008

Affiliations

Center for Nano- and Molecular Science and Technology; Institute for Cellular and Molecular Biology

Physical Chemistry of Biological Interfaces

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. We are interested in these topics for two principal reasons. First, understanding the organization of biological systems is of vital biomedical importance. Second, we seek to exploit the weak but long-range interactions involved in noncovalent organization of biological macromolecules at prepared surfaces and interfaces with the ultimate goal of integrating biological and inorganic materials in a controlled and robust manner.

Research in the Webb group is multidisciplinary and employs a variety of physical and analytical techniques. We study the physical chemistry of electrostatic fields at protein-protein interfaces using vibrational spectroscopy coupled with computational methods; we prepare and characterize chemically modified surfaces that interact specifically with folded, functional proteins using X-ray photoelectron spectroscopy, atomic force microscopy, and surface spectroscopic techniques; and we use biochemical control over the dynamic behavior of cytoskeletal fibers tethered to patterned surfaces and monitored through optical microscopy.

Electrostatic Fields at the Protein-Protein Interface

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. Furthermore, molecules that promote or disrupt specific macromolecular interactions have vast pharmacological potential. Macromolecular interactions lead to emergent properties necessary for life, but can only be studied or understood if the molecular-level, noncovalent, electrostatic forces that drive and control those interactions are themselves understood. The Webb group measures electrostatic fields at protein-protein interfaces and seeks to develop computational models that accurately predict these interactions.

Electrostatic Control of Protein Binding at Surfaces

Incorporation of a protein into a sensing, electronic, or biofuel device often requires that the protein be tethered to an inorganic surface. The Webb group uses surface chemical modification to prepare substrates that present an ideal electrostatic interface for the noncovalent binding of proteins in a controlled and organized manner. We are developing surface chemical functionalization techniques that are completely general to allow controlled binding of any protein of interest, including those of unknown structure or complicated molecular biology.

For further information, please contact Lauren Webb at lwebb@cm.utexas.edu.

 

Representative Publications

Hu, W. and Webb, L. J. "Direct Measurement of the Membrane Dipole Field in Bicelles Using Vibrational Stark Effect Spectroscopy." J. Phys. Chem. Lett 2011, 2, 1925-1930.

Ensign, D.L. and Webb, L. J. "Factors Determining Electrostatic Fields at the Ras/Effector Interface." Proteins 2011, DOI 10.1002/prot.23095 (published online 13 July 2011).

 

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 2010, 26, 18959-18966.

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 2010 114, 15331-15344.

Webb, L. J.; Boxer, S. G. "Electrostatic Fields Near the Active Site of Human Aldose Reductase: 1. New Inhibitors and Vibrational Stark Effect Measurements." Biochemistry 47 (2008): 1588-1598.

Webb, L. J.; Michalak, D. J.; Biteen, J. S.; Brunschwig, B. S.; Chan, A. S. Y.; Knapp, D.W.; Meyer, H. M.; Nemanick, E. J.; Traub, M. C; Lewis, N. S. "High-Resolution Soft X-ray Photoelectron Spectroscopic Studies and Scanning Auger Microscopy Studies of the Air Oxidation of Alkylated Silicon(111) Surfaces." J. Phys. Chem. B 110 (2006): 23450-23459.

Webb, L. J.; Rivillon, S.; Michalak, D. J.; Chabal, Y. J.; Lewis, N. S. "Transmission Infrared Spectroscopy of Methyl- and Ethyl-Terminated Silicon(111) Surfaces." J. Phys. Chem. B 110 (2006): 7349-7356.