David A. Drummond, Ph.D.

Pew.Feature.Scholar.Bio.Title
Assistant Professor
Pew.Feature.Scholar.Bio.Department
Department of Biochemistry and Molecular Biology
Pew.Feature.Scholar.Bio.Institution
University of Chicago
Pew.Feature.Scholar.Bio.Address
929 E 57th St
GCIS W234
Pew.Feature.Scholar.Bio.City, Pew.Feature.Scholar.Bio.State, Pew.Feature.Scholar.Bio.Zip
Chicago, IL 60637
Pew.Feature.Scholar.Bio.Phone
(773) 834-2017
Pew.Feature.Scholar.Bio.Email
[email protected]
Pew.Feature.Scholar.Bio.Website
http://drummond.openwetware.org/
Pew.Feature.Scholar.Bio.ResearchField
Biochemistry; Molecular Biology
Pew.Feature.Scholar.Bio.AwardYear
2012

Research

What are the spectrum, frequency and consequences of errors in protein synthesis? How do cells sense and respond to misfolded proteins, particularly in the eukaryotic cytosol? How does stochasticity in protein synthesis alter the composition and stability of the proteome?

What benefits do errors confer? Does error-induced protein misfolding influence the progression of neurodegenerative diseases such as ALS?

We are pursuing mechanistic answers to these questions, taking a biochemical and genetic approach, with an emphasis on developing high-resolution, high-mass-accuracy mass spectrometric techniques for proteome-scale quantitation. From a theoretical standpoint, we are interested in understanding the imprints that natural selection on fidelity and misfolding leave on evolving genes and genomes.

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