Enhanced protein fold recognition using secondary structure information from NMR
Ayers, Daniel; Gooley, P; Widmer-Cooper, Asaph; Torda, Andrew
NMR offers the possibility of accurate secondary structure for proteins that would be too large for structure determination. In the absence of an X- ray crystal structure, this information should be useful as an adjunct to protein fold recognition methods based on low resolution force fields. The value of this information has been tested by adding varying amounts of artificial secondary structure data and threading a sequence through a library of candidate folds. Using a literature test set,...[Show more]
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