Contact InformationOffice: WEL: 3.212B
LabOffice: WEL 3.306
Chemistry A.B., Bowdoin College, 2000
Ph.D, California Institute of Technology, 2005
NIH Postdoctoral Fellow, Stanford University, 2005-2008
Alfred P. Sloan Research Fellow, 2012
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
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 firstname.lastname@example.org.
Raigoza, A. F. and Webb, L. J. “Molecularly Resolved Images of Peptide-Functionalized Gold Surfaces by Scanning Tunneling Microscopy.” J. Am. Chem. Soc. 2012, 134, 19354-19357.
Schroder, K.; Celio, H.; Webb, L. J.;* Stevenson, K. S.* “Examining Solid Electrolyte Interphase Formation on Crystalline Silicon Electrodes: Influence of Electrochemical Preparation and Ambient Exposure Conditions.” J. Phys. Chem. C 2012, 116, 19737-19747.
Ragain, C. M.; Newberry, R. W.; Ritchie, A. W.; Webb, L. J. “The Role of Electrostatics in
Differential Binding of RalGDS to Rap Mutations E30 and K31E Investigated by Vibrational
Spectroscopy of Thiocyanate Probes.” J. Phys. Chem. B 2012, 116, 9326-9336.
Stafford, A. J.; Walker, D.; Webb, L. J. “Electrostatic Effects of Mutations to Ras Glutamine 61 Measured Using Vibrational Spectroscopy of a Thiocyanate Probe.” Biochemistry 2012, 51, 2757-2767.
Gallardo, I. F. and Webb, L. J. “Demonstration of α-Helical Structure of Peptides Tethered to Gold Surfaces Using Surface Infrared and Circular Dichroic Spectroscopies.” Langmuir 2012, 28, 3510-3515.
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, 79, 3511-3524.