Cotranslational Protein Folding and Terminus Hydrophobicity
نویسندگان
چکیده
منابع مشابه
Cotranslational Protein Folding and Terminus Hydrophobicity
Peptides fold on a time scale that is much smaller than the time required for synthesis, whence all proteins potentially fold cotranslationally to some degree (followed by additional folding events after release from the ribosome). In this paper, in three different ways, we find that cotranslational folding success is associated with higher hydrophobicity at the N-terminus than at the C-terminu...
متن کاملCotranslational protein folding.
The problem of how the linear amino acid sequence of a polypeptide folds to assume its unique tertiary structure is one of the most basic and challenging conundrums of contemporary science. Many of the principles and characteristics of protein folding have been learned by studying refolding of denatured polypeptides. However, the problem of protein folding cannot be completely understood withou...
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Key words Classification system and/or index terms (if any) Supplementary bibliographical information Language ISSN and key title ISBN Recipient's notes Number of pages Price Security classification Distribution by (name and address) I, the undersigned, being the copyright owner of the abstract of the above-mentioned dissertation, hereby grant to all reference sources the permission to publish ...
متن کاملEnergy landscape theory for cotranslational protein folding
Abstract Energy landscape theory describes how a full-length protein can attain its native fold after sampling only a tiny fraction of all possible structures. Although protein folding is now understood to be concomitant with synthesis on the ribosome there have been few attempts to modify energy landscape theory by accounting for cotranslational folding. This paper introduces a model for cotra...
متن کاملCotranslational protein folding - fact or fiction?
MOTIVATION Experimentalists have amassed extensive evidence over the past four decades that proteins appear to fold during production by the ribosome. Protein structure prediction methods, however, do not incorporate this property of folding. A thorough study to find the fingerprint of such sequential folding is the first step towards using it in folding algorithms, so assisting structure predi...
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ژورنال
عنوان ژورنال: Advances in Bioinformatics
سال: 2011
ISSN: 1687-8027,1687-8035
DOI: 10.1155/2011/176813