Directionality in protein fold prediction

10 years 6 months ago
Directionality in protein fold prediction
Background: Ever since the ground-breaking work of Anfinsen et al. in which a denatured protein was found to refold to its native state, it has been frequently stated by the protein fold prediction community that all the information required for protein folding lies in the amino acid sequence. Recent in vitro experiments and in silico computational studies, however, have shown that cotranslation may affect the folding pathway of some proteins, especially those of ancient folds. In this paper aspects of cotranslational folding have been incorporated into a protein structure prediction algorithm by adapting the Rosetta program to fold proteins as the nascent chain elongates. This makes it possible to conduct a pairwise comparison of folding accuracy, by comparing folds created sequentially from each end of the protein. Results: A single main result emerged: in 94% of proteins analyzed, following the sense of translation, from N-terminus to C-terminus, produced better predictions than fo...
Jonathan J. Ellis, Fabien P. E. Huard, Charlotte M
Added 12 May 2011
Updated 12 May 2011
Type Journal
Year 2010
Authors Jonathan J. Ellis, Fabien P. E. Huard, Charlotte M. Deane, Sheenal Srivastava, Graham R. Wood
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