NMR detection of side chain-side chain hydrogen bonding interactions in 13C/15N-labeled proteins Journal Article
| Authors: | Liu, A.; Hu, W.; Majumdar, A.; Rosen, M. K.; Patel, D. J. |
| Article Title: | NMR detection of side chain-side chain hydrogen bonding interactions in 13C/15N-labeled proteins |
| Abstract: | 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 15N(ε) of arginine 71, which serves as the hydrogen donor, and the acceptor carboxylate carbon 13CO2(γ) of aspartate 100 in a 12 kDa protein, human FKBP12, is detected via the trans-hydrogen bond (3h)J(NεCO2γ) coupling by employing a novel HNCO-type experiment, soft CPD-HNCO. The (3h)J(NεCO2γ) coupling constant appears to be even smaller than the average value of backbone (3h)J(NC') couplings, consistent with more extensive local dynamics in protein side chains. The identification of trans-hydrogen bond J-couplings between protein side chains should provide useful markers for monitoring hydrogen bonding interactions that contribute to the stability of protein folds, to alignments within enzyme active sites and to recognition events at macromolecular interfaces. |
| Keywords: | proteins; animals; isotope labeling; molecular recognition; nuclear magnetic resonance spectroscopy; hydrogen bond; hydrogen bonding; cattle; protein folding; protein structure; structure analysis; m protein; protein structure, secondary; aspartic acid; nitrogen; arginine; carbon; carbon isotopes; nitrogen isotopes; enzyme active site; nuclear magnetic resonance, biomolecular; guanidine; humans; human; priority journal; article; tacrolimus binding protein 1a; fkbp12; sensitivity enhancement; nmr detection; side chain-side chain hydrogen bonds |
| Journal Title: | Journal of Biomolecular NMR |
| Volume: | 17 |
| Issue: | 4 |
| ISSN: | 0925-2738 |
| Publisher: | Springer |
| Date Published: | 2000-08-01 |
| Start Page: | 305 |
| End Page: | 310 |
| Language: | English |
| DOI: | 10.1023/a:1008390813387 |
| PUBMED: | 11014594 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 18 November 2015 -- Source: Scopus |
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