Druggable protein interaction sites are more predisposed to surface pocket formation than the rest of the protein surface.
Submitted by Anonymous on Sat, 2015-03-21 18:34
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Other Rosetta Papers
Selectivity by small-molecule inhibitors of protein interactions can be driven by protein surface fluctuations.
Submitted by Anonymous on Sat, 2015-03-21 18:31
Simple physical models connect theory and experiment in protein folding kinetics.
Submitted by Anonymous on Sun, 2015-03-15 06:45
A Ras-induced conformational switch in the Ras activator Son of sevenless.
Submitted by Anonymous on Sun, 2015-03-15 06:45
Contrasting roles for symmetrically disposed beta-turns in the folding of a small protein.
Submitted by Anonymous on Sun, 2015-03-15 06:45
Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions.
Submitted by Anonymous on Sun, 2015-03-15 06:45
Prediction of local structure in proteins using a library of sequence-structure motifs.
Submitted by Anonymous on Sun, 2015-03-15 06:45
The single helix in protein L is largely disrupted at the rate-limiting step in folding.
Submitted by Anonymous on Sun, 2015-03-15 06:45
Contributions of solvent-solvent hydrogen bonding and van der Waals interactions to the attraction between methane molecules in water.
Submitted by Anonymous on Sun, 2015-03-15 06:45
Clustering of low-energy conformations near the native structures of small proteins.
Submitted by Anonymous on Sun, 2015-03-15 06:45