Backrub-like backbone simulation recapitulates natural protein conformational variability and improves mutant side-chain prediction.
Submitted by Anonymous on Sun, 2015-03-15 06:45
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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 Sun, 2015-03-15 06:45
Prediction of protein-protein interface sequence diversity using flexible backbone computational protein design.
Submitted by Anonymous on Sun, 2015-03-15 06:45
Multi-constraint computational design suggests that native sequences of germline antibody H3 loops are nearly optimal for conformational flexibility.
Submitted by Anonymous on Sun, 2015-03-15 06:45
A correspondence between solution-state dynamics of an individual protein and the sequence and conformational diversity of its family.
Submitted by Anonymous on Sun, 2015-03-15 06:45
Sub-angstrom accuracy in protein loop reconstruction by robotics-inspired conformational sampling.
Submitted by Anonymous on Sun, 2015-03-15 06:45
Backbone flexibility in computational protein design.
Submitted by Anonymous on Sun, 2015-03-15 06:45
Computer-aided design of functional protein interactions.
Submitted by Anonymous on Sun, 2015-03-15 06:45
RosettaBackrub--a web server for flexible backbone protein structure modeling and design.
Submitted by Anonymous on Sun, 2015-03-15 06:45
Structure-based prediction of the peptide sequence space recognized by natural and synthetic PDZ domains.
Submitted by Anonymous on Sun, 2015-03-15 06:45