Home
People
Publications
Research
Meetings
News
Contact Us

We are part of:
Department of Bioengineering and Therapeutic Sciences
California Institute for Quantitative Biosciences (QB3)
Integrative Program in Quantitative Biology
Graduate Group in Biophysics
Graduate Program in Bioinformatics
Graduate Program in Chemistry and Chemical Biology (CCB)
Graduate Program in Pharmaceutical Sciences and Pharmacogenomics (PSPG)
NIH Center for Protein Folding Machinery
NIH Center on "Engineering Cellular Control: Synthetic Signaling and Motility Systems"
Synthetic Biology Engineering and Research Center (SynBERC)
We are located at:
UCSF QB3
1700 4th Street, Byers Hall
San Francisco, CA 94143-2540
(CA 94158 for courier delivery)
401 (computational lab)
409 (experimental lab)
408 B (Tanja Kortemme's office)


Group Photo We are interested in how biological molecules communicate with each other, and how this communication encodes the processing of information. How do biomolecules recognize one another, and how do their interactions transduce signals? How do molecules build up "modules" that act as "adaptors", "switches" and feedback-loops? How are modules wired together into the networks responsible for regulation and decision processes observed in biology?

Computationally, we have developed a simple physical energy function for the prediction and design of protein-protein interactions, at the atomic level. Experimentally, we have applied this model to the computational redesign of a protein interface and have created an artificial DNA binding protein with new specificity. More recently, we have developed a computational strategy for the redesign of protein complexes to generate new pairs of interacting proteins.

We are now applying and extending our computational model at different "resolution", ranging from details of atom-atom interactions to cellular communication networks. We are aiming to develop more accurate methods to model the structural details of molecular interactions. Can new interactions and modules with defined properties be engineered? Ultimately we would like to apply computational and experimental methods to better understand how cellular processes are regulated by molecular communication.



Selected publications

Oberdorf R, Kortemme T. Complex topology rather than complex membership is a determinant of protein dosage sensitivity. Mol Syst Biol. 2009;5:253.

Friedland GD, Lakomek NA, Griesinger C, Meiler J, Kortemme T. A correspondence between solution-state dynamics of an individual protein and the sequence and conformational diversity of its family. PLoS Comput Biol. 2009 May;5(5):e1000393.

Humphris EL, Kortemme T. (2008). Prediction of protein-protein interface sequence diversity using flexible backbone computational protein design. Structure. Dec 12;16(12):1777-88.

Smith CA and Kortemme T. (2008). Backrub-like backbone simulation recapitulates natural protein conformational variability and improves mutant side-chain prediction. J Mol Biol. 380(4):742-56.

Eames M and Kortemme T. (2007). Structural Mapping of Protein Interactions Reveals Differences in Evolutionary Pressures Correlated to mRNA Level and Protein Abundance. Structure 15, 1442-1451.

Humphris EL and Kortemme T. Design of multi-specificity in protein interfaces. (2007). PLoS Comput Biol. 3(8): 1591-1604.

Kortemme, T. and D. Baker. (2004). Computational design of protein-protein interactions. Curr Opin Chem Biol 8(1): 91-7. (review)