Dear crystallographers - I've been trying without success to find a suitable system to test a method for predicting change in binding energy (delta-delta-G) due to mutations of protein-protein complexes that result in a change in net charge. In particular I'm looking for a system with the following features for a single mutation:
* crystal structures and experimental binding affinity data available for both wild-type and mutant complexes * net change of charge of ±1 upon mutation (i.e. charged residue to neutral or vice versa--I'm not considering charge flipping at the moment) * non-trivial conformational change in the region around the mutated residue If you happen to know of any systems that may qualify, I would appreciate any information you could send my way. Thank you! Cheers, Jared -- Jared Sampson Ph.D. Candidate Honig/Shapiro and Friesner Labs Columbia University New York, NY
