NMR paper Detection of very weak side chain-main chain hydrogen bonding interactions in medium-

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[NMR paper] Detection of very weak side chain-main chain hydrogen bonding interactions in medium-

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Side-chains:

NOEs:

Structure from NMR restraints:

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Fragment-based:

Rosetta-NMR (Robetta)

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Amber

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Promega- Proline

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TALOS

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d2D

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11-18-2010, 09:15 PM

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Detection of very weak side chain-main chain hydrogen bonding interactions in medium-

Detection of very weak side chain-main chain hydrogen bonding interactions in medium-size 13C/15N-labeled proteins by sensitivity-enhanced NMR spectroscopy.

Related Articles Detection of very weak side chain-main chain hydrogen bonding interactions in medium-size 13C/15N-labeled proteins by sensitivity-enhanced NMR spectroscopy.

J Biomol NMR. 2000 May;17(1):79-82

Authors: Liu A, Hu W, Majumdar A, Rosen MK, Patel DJ

We describe the direct observation of very weak side chain-main chain hydrogen bonding interactions in medium-size 13C/15N-labeled proteins with sensitivity-enhanced NMR spectroscopy. Specifically, the remote correlation. between the hydrogen acceptor side chain carboxylate carbon 13CO2delta of glutamate 54 and the hydrogen donor backbone amide 15N of methionine 49 in a 12 kDa protein, human FKBP12, is detected via the trans-hydrogen bond 3hJ(NCO2delta) coupling by employing a novel sensitivity-enhanced HNCO-type experiment, CPD-HNCO. The 3hJ(NCO2delta) coupling constant appears to be even smaller than the average value of backbone 3hJ(NC') couplings, consistent with more extensive local dynamics in protein side chains.

PMID: 10909868 [PubMed - indexed for MEDLINE]

Source: PubMed

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