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Robert Nakamoto

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Associate Director

Robert Nakamoto is a Professor in the Department of Molecular Physiology and Biological Physics. The Nakamoto laboratory uses biochemical, kinetic, thermodynamic and biophysical approaches to elucidate the structure-function relationships of coupling mechanisms of active transporters. Currently, they are focused on the molecular mechanisms of the P-type ion transporting ATPases, the ABC-type multiple drug resistance transporters, the FOF1 ATP synthase and the TonB-dependent outer membrane iron transporters. They specialize in functional expression of proteins in native membranes and develop methods to measure transport activity in whole cells, membrane vesicles or reconstituted systems. They use mutagenic and chemical modification approaches to modulate reaction steps of transport mechanisms. In particular, they have exploited intramolecular disulfides to stabilize transport active conformations that cannot otherwise be trapped. They also use cysteine scanning for placement of spectroscopic probes to explore protein dynamics and conformational shifts during transport cycles. Of interest to the Institute of Global Infectious Disease are the multiple drug resistance transporter, which also appear in pathogenic bacteria, and the outer membrane transporters which are recognized by host immune responses and act as the receptor and import pathways for colicins and bacterial phages.