Arvind Kannan

Hertz Fellow: Arvind Kannan
School

California Institute of Technology

Area of Study

Chemical Engineering

Fellowship Years

2012 - present

Arvind Kannan is a graduate student in chemical engineering at Stanford University. He holds a BS in chemical engineering from the California Institute of Technology and an MPhil in chemistry from the University of Cambridge, where he was a Churchill Scholar.

Arvind is passionate about leveraging recent advances in high-throughput biology towards the study and manipulation of sequence-function relationships in proteins. To this end, his research at Stanford thus far has focused on the development of a new biotechnology platform, which enables massively parallel, quantitative biochemical and biophysical measurements on millions of protein variants expressed from yeast or bacteria. Built around high-density microcapillary arrays and a precise laser-based extraction method, this platform has enabled the high-throughput analysis of individual cells and their protein products via a variety of fluorescent assays, followed by facile recovery of clones of interest for future characterization. Arvind is now applying this technology towards a number of both fundamental and applied protein engineering studies, including an exploration of substrate specificity within the alkaline phosphatase enzyme superfamily and the engineering of peptide toxins from animal venoms as selective sodium channel inhibitors.

Arvind is a co-author on five publications and has won numerous academic awards, including an Amgen Scholarship and an ACS Best of BIOT Award. Past research highlights include the design of a cytochrome P450 enzyme that can directly insert reactive carbene groups into carbon-carbon bonds (Caltech), the establishment of a computational drug discovery pipeline based on the identification of transient binding pockets in long-timescale molecular dynamics simulations of drug targets (D.E. Shaw Research), and the use of NMR chemical shift measurements to study the dynamics of intrinsically disordered or highly flexible protein domains (Cambridge).