You are here

Home

Kortemme

Institute: 
University of California, San Francisco
Machine name: 
kortemme
PI NCBI name: 
Kortemme T
PI email: 
kortemme@cgl.ucsf.edu

A simple model of backbone flexibility improves modeling of side-chain conformational variability

Submitted by Anonymous on Fri, 2010-11-12 04:39
Authors: 
Friedland, G. D., Linares, A. J., Smith, C. A. and Kortemme, T.
Volume: 
380
Link to Article: 
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citati...
Year: 
2008
Reference: 
J Mol Biol
Pages: 
757-774
Lab: 
Kortemme
Publication Type: 
Method
Publication Subject: 
Other Rosetta Papers

Prediction of protein-protein interface sequence diversity using flexible backbone computational protein design

Submitted by Anonymous on Fri, 2010-11-12 04:39
Authors: 
Humphris, E. L. and Kortemme, T.
Volume: 
16
Link to Article: 
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citati...
Year: 
2008
Reference: 
Structure
Pages: 
1777-1788
Lab: 
Kortemme
Publication Type: 
Method
Publication Subject: 
Other Rosetta Papers

Backrub-like backbone simulation recapitulates natural protein conformational variability and improves mutant side-chain prediction

Submitted by Anonymous on Fri, 2010-11-12 04:39
Authors: 
Smith, C. A. and Kortemme, T.
Volume: 
380
Link to Article: 
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citati...
Year: 
2008
Reference: 
J Mol Biol
Pages: 
742-756
Lab: 
Kortemme
Publication Type: 
Method
Publication Subject: 
Other Rosetta Papers

Designing ensembles in conformational and sequence space to characterize and engineer proteins

Submitted by Anonymous on Fri, 2010-11-12 04:39
Authors: 
Friedland, G. D. and Kortemme, T.
Link to Article: 
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citati...
Year: 
2010
Reference: 
Curr Opin Struct Biol
Publication Type: 
Review
Publication Subject: 
Other Rosetta Papers
Lab: 
Kortemme

Multi-constraint computational design suggests that native sequences of germline antibody H3 loops are nearly optimal for conformational flexibility

Submitted by Anonymous on Fri, 2010-11-12 04:39
Authors: 
Babor, M. and Kortemme, T.
Volume: 
75
Link to Article: 
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citati...
Year: 
2009
Reference: 
Proteins
Pages: 
846-858
Lab: 
Kortemme
Publication Type: 
Method
Publication Subject: 
Other Rosetta Papers

A correspondence between solution-state dynamics of an individual protein and the sequence and conformational diversity of its family

Submitted by Anonymous on Fri, 2010-11-12 04:39
Authors: 
Friedland, G. D., Lakomek, N. A., Griesinger, C., Meiler, J. and Kortemme, T.
Volume: 
5
Link to Article: 
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citati...
Year: 
2009
Reference: 
PLoS Comput Biol
Pages: 
e1000393
Lab: 
Kortemme
Publication Type: 
Method
Publication Subject: 
Other Rosetta Papers

Sub-angstrom accuracy in protein loop reconstruction by robotics-inspired conformational sampling

Submitted by Anonymous on Fri, 2010-11-12 04:39
Authors: 
Mandell, D. J., Coutsias, E. A. and Kortemme, T.
Volume: 
6
Link to Article: 
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citati...
Year: 
2009
Reference: 
Nat Methods
Pages: 
551-552
Lab: 
Kortemme
Publication Type: 
Method
Publication Subject: 
Other Rosetta Papers

Pages