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Evaluation of current techniques for Ab initio protein structure prediction
Author(s) -
Defay Tom,
Cohen Fred E.
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340230317
Subject(s) - protein structure prediction , casp , contest , protein structure , computer science , motif (music) , protein tertiary structure , computational biology , ab initio , structural motif , data mining , chemistry , biology , physics , biochemistry , organic chemistry , political science , law , acoustics
The results of a protein structure prediction contest are reviewed. Twelve different groups entered predictions on 14 proteins of known sequence whose structures had been determined but not yet disseminated to the scientific community. Thus, these represent true tests of the current state of structure prediction methodologies. From this work, it is clear that accurate tertiary structure prediction is not yet possible. However, protein fold and motif prediction are possible when the motif is recognizably similar to another known structure. Internal symmetry and the information inherent in an aligned family of homologous sequences facilitate predictive efforts. Novel folds remain a major challenge for prediction efforts. © 1995 Wiley‐Liss, Inc.