Scholars@Duke
Terrence Gilbert Oas

Terrence Gilbert Oas

Professor of Biochemistry
Biochemistry
oas@duke.edu
Duke Box 3711, Durham, NC 27710
230C Nanaline Duke, Durham, NC 27710

Overview

Our laboratory is primarily interested in the mechanisms of protein folding. We use nuclear magnetic resonance (NMR) and other types of spectroscopy to study the solution structure, stability and folding reactions of small protein models. These include monomeric λ repressor, the B domain of protein A (BdpA) and various regulator of G-protein signalling (RGS) domains. Our biophysical studies are used to inform our investigations of the role of folding mechanism in the function of proteins in the cell. For example, a naturally occuring cancer-causing mutation in the RGS domain of axin appears to lower the thermodynamic stability of the domain. We are developing methods to compensate for such destabilizing mutations, thereby restoring normal function to the protein.We are also developing computational models of protein folding as a way to better understand the mechanisms and as a tool in the design of new experiments.

Current Appointments & Affiliations

Professor of Biochemistry · 2011 - Present Biochemistry, Basic Science Departments
Professor of Chemistry · 2024 - Present Chemistry, Trinity College of Arts & Sciences

In the News

Published April 15, 2022
School of Medicine Celebrates 2022 Faculty Achievement Awards

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Recent Publications

Efficient enumeration and visualization of helix-coil ensembles.

Journal Article Biophys J · February 6, 2024 Helix-coil models are routinely used to interpret circular dichroism data of helical peptides or predict the helicity of naturally-occurring and designed polypeptides. However, a helix-coil model contains significantly more information than mean helicity a ... Full text Link to item Cite

Efficient Enumeration and Visualization of Helix-coil Ensembles.

Journal Article bioRxiv · September 17, 2023 Helix-coil models are routinely used to interpret CD data of helical peptides or predict the helicity of naturally-occurring and designed polypeptides. However, a helix-coil model contains significantly more information than mean helicity alone, as it defi ... Full text Open Access Link to item Cite
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Recent Grants

Bioinformatics and Computational Biology Training Program

Inst. Training Prgm or CMEMentor · Awarded by National Institutes of Health · 2005 - 2021

Role of protein A structure, folding kinetics and dynamics in S. aureus virulence

ResearchPrincipal Investigator · Awarded by National Institutes of Health · 2016 - 2021

Organization and Function of Cellular Structure

Inst. Training Prgm or CMEMentor · Awarded by National Institutes of Health · 1975 - 2020

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Education, Training & Certifications

University of Oregon · 1986 Ph.D.

External Links

Oas Lab Web Site