Abstract
Proteins frequently adopt similar three-dimensional folds even if there is no detectable homology on the sequence level. Therefore, it is likely that a substantial fraction of known sequences will have native folds which resemble some known structure. The task of fold recognition is to identify such coincidences, thereby predicting the unknown folds of known amino acid sequences. We present the principles of a fold recognition technique based on mean force potentials and apply the procedure in two case studies, demonstrating that the method is able to recognize native-like sequence structure pairs in cases where no significant sequence homology is detectable.
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Sippl, M.J., Weitckus, S., Flöckner, H. (1995). Fold Recognition. In: Pullman, A., Jortner, J., Pullman, B. (eds) Modelling of Biomolecular Structures and Mechanisms. The Jerusalem Symposia on Quantum Chemistry and Biochemistry, vol 27. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-0497-5_10
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DOI: https://doi.org/10.1007/978-94-011-0497-5_10
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