
Ian K. Webb
Associate Professor · Bioanalytical Chemistry
Indiana University–Purdue University IndianapolisAbout
Ian K. Webb is an Associate Professor in the Department of Chemistry and Chemical Biology at Indiana University Indianapolis, leading the Webb Lab which develops advanced mass spectrometry tools for structural biology of dynamic and disordered proteins. His research leverages ion mobility and gas-phase ion/ion chemistry to overcome limitations of traditional biophysical techniques.
Webb earned his B.S. from The College of William and Mary (2008) and Ph.D. from Purdue University (2012), followed by postdoctoral training at Pacific Northwest National Laboratory under Richard Smith.
His primary research focuses on covalent footprinting, crosslinking, and electrostatic reaction methodologies using mass spectrometry to study protein folding, proteoforms, and protein-protein interactions. Key applications target human disease mechanisms and cellular function, particularly for intrinsically disordered proteins where conventional structural methods fail. The lab emphasizes the 'three S's' of mass spectrometry: sensitivity, speed, and selectivity.
Recent publications reveal a strong trend toward gas-phase structural proteomics, with innovations in ion/ion reaction kinetics, mobility-based separation, and multi-length crosslinker applications. Work spans method development (e.g., duel electrospray systems) to biological applications like α-synuclein conformational analysis.
Scientific recognition includes:
- NSF CAREER Award for gas-phase structural methodology development
Webb mentors five active graduate students (Gurav, Renbarger, Black, Dollar, Cain) and a postdoc (Davis), with past advisees including MS graduate Sexton and multiple undergraduates. His research is supported by the NSF CAREER Award and NIH MIRA grant focused on proteoform-structure relationships in disordered systems.
The Webb Lab operates as an interdisciplinary team combining chemical labeling, native/top-down proteomics, and computational modeling to resolve impacts of proteoforms on protein system structure-function relationships.
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