CI2Daggett Research Group

University of Washington - College of Engineering - School of Medicine - Department of Bioengineering

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Paper of the Month

A temperature-dependent conformational change of NADH oxidase from Thermus thermophilus HB8
Paper of the Month
Merkley E.D., Daggett V., and Parson W.W.
Prot Struct Func Bioinf 80: 546-555, 2012

Using molecular dynamics simulations and steady-state fluorescence spectroscopy, we have identified a conformational change in the active site of a thermophilic flavoenzyme, NADH oxidase from Thermus thermophilus HB8 (NOX). The enzyme's far-UV circular dichroism spectrum, intrinsic tryptophan fluorescence, and apparent molecular weight measured by dynamic light scattering varied little between 25 and 75°C. More...


Goals: Realistic simulation of protein dynamics, unfolding/folding, and conformational transitions linked to disease.

Protein Simulation and Analysis

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