A simple physical model for binding energy hot spots in protein–protein complexes

Por Kortemme, Tanja, Baker, David
Publicado em 2002

Genome-wide structural mapping of protein interactions reveals differences in abundance-and expression-dependent evolutionary pressures

Por Eames, Matt, Kortemme, Tanja
Publicado em 2007

Complex topology rather than complex membership is a determinant of protein dosage sensitivity

Por Oberdorf, Richard, Kortemme, Tanja
Publicado em 2009

Improvements to Robotics-Inspired Conformational Sampling in Rosetta

Por Stein, Amelie, Kortemme, Tanja
Publicado em 2013

Computational Protein Design Quantifies Structural Constraints on Amino Acid Covariation

Por Ollikainen, Noah, Kortemme, Tanja
Publicado em 2013

Multi-constraint Computational Design Suggests that Native Sequences of Germline Antibody H3 Loops are Nearly Optimal for Conformational Flexibility

Por Babor, Mariana, Kortemme, Tanja
Publicado em 2009

Design of Multi-Specificity in Protein Interfaces

Por Humphris, Elisabeth L, Kortemme, Tanja
Publicado em 2007

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

Por Smith, Colin A., Kortemme, Tanja
Publicado em 2008

Predicting the Tolerated Sequences for Proteins and Protein Interfaces Using RosettaBackrub Flexible Backbone Design

Por Smith, Colin A., Kortemme, Tanja
Publicado em 2011

Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions.

Por Chakrabartty, A., Kortemme, T., Baldwin, R. L.
Publicado em 1994

Assessment of flexible backbone protein design methods for sequence library prediction in the therapeutic antibody Herceptin–HER2 interface

Por Babor, Mariana, Mandell, Daniel J, Kortemme, Tanja
Publicado em 2011

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

Por Mandell, Daniel J, Coutsias, Evangelos A, Kortemme, Tanja
Publicado em 2009

Coupling Protein Side-Chain and Backbone Flexibility Improves the Re-design of Protein-Ligand Specificity

Por Ollikainen, Noah, de Jong, René M., Kortemme, Tanja
Publicado no PLoS Comput Biol (2015)

Close agreement between the orientation dependence of hydrogen bonds observed in protein structures and quantum mechanical calculations

Por Morozov, Alexandre V., Kortemme, Tanja, Tsemekhman, Kiril, Baker, David
Publicado em 2004

Methods in Enzymology: “Flexible backbone sampling methods to model and design protein alternative conformations”

Por Ollikainen, Noah, Smith, Colin A., Fraser, James S., Kortemme, Tanja
Publicado em 2013

Design of a Photoswitchable Cadherin

Por Ritterson, Ryan S., Kuchenbecker, Kristopher M., Michalik, Michael, Kortemme, Tanja
Publicado em 2013

Reprogramming an ATP-driven protein machine into a light-gated nanocage

Por Hoersch, Daniel, Roh, Soung-Hun, Chiu, Wah, Kortemme, Tanja
Publicado em 2013

Design of Light-Controlled Protein Conformations and Functions

Por Ritterson, Ryan S., Hoersch, Daniel, Barlow, Kyle A., Kortemme, Tanja
Publicado no Methods Mol Biol (2016)

A new hydrogen-bonding potential for the design of protein–RNA interactions predicts specific contacts and discriminates decoys

Por Chen, Yu, Kortemme, Tanja, Robertson, Tim, Baker, David, Varani, Gabriele
Publicado em 2004

Quantification of the transferability of a designed protein specificity switch reveals extensive epistasis in molecular recognition

Por Melero, Cristina, Ollikainen, Noah, Harwood, Ian, Karpiak, Joel, Kortemme, Tanja
Publicado em 2014