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Structural dependencies of protein backbone 2JNC' couplings.

ABSTRACT: Protein folding can introduce strain in peptide covalent geometry, including deviations from planarity that are difficult to detect, especially for a protein in solution. We have found dependencies in protein backbone (2)J(NC') couplings on the planarity and the relative orientation of the sequential peptide planes. These dependences were observed in experimental (2)J(NC') couplings from seven proteins, and also were supported by DFT calculations for a model tripeptide. Findings indicate that elevated (2)J(NC') couplings may serve as reporters of structural strain in the protein backbone imposed by protein folds. Such information, supplemented with the H-bond strengths derived from (h3)J(NC') couplings, provides useful insight into the overall energy profile of the protein backbone in solution.

SUBMITTER: Juranic N

PROVIDER: S-EPMC2271174 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature

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Structural dependencies of protein backbone 2JNC' couplings.

Juranić Nenad N Dannenberg J J JJ Cornilescu Gabriel G Salvador Pedro P Atanasova Elena E Ahn Hee-Chul HC Macura Slobodan S Markley John L JL Prendergast Franklyn G FG

Protein science : a publication of the Protein Society 20080227 4

Protein folding can introduce strain in peptide covalent geometry, including deviations from planarity that are difficult to detect, especially for a protein in solution. We have found dependencies in protein backbone (2)J(NC') couplings on the planarity and the relative orientation of the sequential peptide planes. These dependences were observed in experimental (2)J(NC') couplings from seven proteins, and also were supported by DFT calculations for a model tripeptide. Findings indicate that el ...[more]

PMID: 18305196

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