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Paper of the Month
A temperature-dependent conformational change of NADH oxidase from Thermus thermophilus HB8
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.
Latest News
- Undergrads interested in conducting research in the Daggett Lab over the summer will only be considered through established UW programs, such as the NNIN REU, Amgen Scholars Program, NASA Internships, and NSF Pathways to Science. Note that these programs have quickly approching deadlines.
- Undergraduate Robert Su received a prestigious Capstone Scholarship from the Department of Bioengineering as well as a Mary Gates Research Scholarship for his Capstone Project work on DIVE. DIVE is a piece of software currently under development in the Daggett Lab for visualizing large datasets. Congratulations, Robert!
- The group's work on urea denaturation was referenced in an article on protein unfolding published by the Royal Society of Chemistry.
- Valerie is honored to have been named a Biophysical Society Fellow for 2011 for her technical innovations and improvements in the field of molecular dynamics simulation.
- The Group is looking for a postdoctoral fellow interested in applying for the UW Sackler Scholars Program. The program offers a competitve two-year fellowship for work in two different labs at UW in the field of biophysics.
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