Stoddard, Barry

Faculty Profile

First Name: 
Last Name: 
[field_fname-formatted] [field_lname-formatted]
Primary Institution: 
Basic Sciences
Mail/Box #: 


Office Location: 

B3-169, FHCRC

Office Phone: 
(206) 667-4031
Alternate Phone: 
(206) 667-4066

Research Summary: 

The overall goal of our laboratory is to characterize the structure/function relationships of a variety of enzymatic catalysts at the atomic level. The results of this work are being extended to engineer novel properties onto existing enzyme scaffolds. Most of our particular area of focus is on enzymes that act to modify nucleic acid substrates, and a unifying theme between many of the individual projects is the selection and engineering of these enzymes for targeted genetic applications. The tools employed by our lab are X-ray crystallography, computer modeling, and genetic manipulation of the molecules of interest, combined with biochemical analyses of function.


1. Structure, function and engineering of intron-encoded homing endonucleases, related rare-cutting endonucleases such as TAL effectors and TAL nucleases and closely related 'domesticated' proteins (intron splicing factors, restriction endonucleases, and genetic regulators)

2. Structure, function and engineering of nucleotide synthesis and salvage enzymes and related enzymology projects.

3. Computational design of novel protein folds, interactions and  functions (with David Baker at UW, Phil Bradley at FHCRC, and Justin Siegel at UC-Davis)

Short Research Description: 
Structure, mechanism and engineering of proteins
Areas of Interest: 
Molecular Structure & Computational Biology
<p> antibiotics, biochemistry, biology cellular, biology, developmental or evolutionary, biophysics, chemotherapeutic agents, computermodeling, crystallography, drug design, genetic manipulation, genetics, pharmacology, physiology, human, active site, chemical cleavage, chemical kinetics, chemical model, cofactor, computer simulation, conformation, Endonuclease, enzyme complex, enzyme inhibitor, enzyme mechanism, enzyme structure, enzyme substrate complex, flash photolysis, Homing endonuclease, isocitrate dehydrogenase, Laue Diffraction, ligand, mutant, nadh phosphate, nucleic acid structure, ribozyme, structural biology, tetrahydrofolate, time resolved data, tricarboxylate, x ray crystallography</p>

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