Addition of side-chain interactions to 310-helix/coil and α-helix/310-helix/coil theory
نویسندگان
چکیده
منابع مشابه
Discovering Side-Chain Correlation in α-Helices
Using a new representation for interactions in protein sequences based on correlations between pairs of amino acids, we have examined α-helical segments from known protein structures for important interactions. Traditional techniques for representing protein sequences usually make an explicit assumption of conditional independence of residues in the sequences. Protein structure analyses, howeve...
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The intrinsic conformational biases of individual amino acids and their interstrand side-chain-side-chain (SC-SC) interactions both contribute to the stability of beta-sheets. The relative magnitudes of these effects have been difficult to assess in the context of folded proteins, where tertiary contacts complicate the quantitative analysis of local effects. We now report the results of such an...
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We describe the direct observation of side chain-side chain hydrogen bonding interactions in proteins with sensitivity-enhanced NMR spectroscopy. Specifically, the remote correlation between the guanidinium nitrogen 15Nepsilon of arginine 71, which serves as the hydrogen donor, and the acceptor carboxylate carbon 13CO2gamma of aspartate 100 in a 12 kDa protein, human FKBP12, is detected via the...
متن کاملProtein contacts, inter-residue interactions and side-chain modelling.
Three-dimensional structures of proteins are the support of their biological functions. Their folds are stabilized by contacts between residues. Inner protein contacts are generally described through direct atomic contacts, i.e. interactions between side-chain atoms, while contact prediction methods mainly used inter-Calpha distances. In this paper, we have analyzed the protein contacts on a re...
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ژورنال
عنوان ژورنال: Protein Science
سال: 1998
ISSN: 0961-8368,1469-896X
DOI: 10.1002/pro.5560071114