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  • sensitivity enhancement  (2)
  • Biochemistry and Biotechnology  (1)
  • Multidimensional NMR  (1)
  • 1
    Electronic Resource
    Electronic Resource
    NMR detection of side chain–side chain hydrogen bonding interactions in 13C/15N-labeled proteins (2000)
    Springer
    Journal of biomolecular NMR 17 (2000), S. 305-310 
    Details
    ISSN: 1573-5001
    Keywords: FKBP12 ; NMR detection ; sensitivity enhancement ; side chain–side chain hydrogen bonds
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: 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 15Nε 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 Nε CO2γ coupling by employing a novel HNCO-type experiment, soft CPD-HNCO. The 3h J Nε CO2γ 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008390813387
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  • 2
    Electronic Resource
    Electronic Resource
    Detection of very weak side chain–main chain hydrogen bonding interactions in medium-size 13C/15N-labeled proteins by sensitivity-enhanced NMR spectroscopy (2000)
    Springer
    Journal of biomolecular NMR 17 (2000), S. 79-82 
    Details
    ISSN: 1573-5001
    Keywords: FKBP12 ; NMR detection ; sensitivity enhancement ; side chain–main chain hydrogen bonds
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract 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 13CO2 δ 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 3h J NCO2δ coupling by employing a novel sensitivity-enhanced HNCO-type experiment, CPD-HNCO. The 3h J NCO2δ 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008373501591
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  • 3
    Electronic Resource
    Electronic Resource
    An (H)C(CO)NH-TOCSY pulse scheme for sequential assignment of protonated methyl groups in otherwise deuterated 15N, 13C-labeled proteins (1996)
    Springer
    Journal of biomolecular NMR 8 (1996), S. 351-356 
    Details
    ISSN: 1573-5001
    Keywords: (H)C(CO)NH-TOCSY ; Multidimensional NMR ; Deuteration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A biosynthetic strategy has recently been developed for the production of 15N, 13C, 2H-labeled proteins using 1H3C-pyruvate as the sole carbon source and D2O as the solvent. The methyl groups of Ala, Val, Leu and Ile (γ2 only) remain highly protonated, while the remaining positions in the molecule are largely deuterated. An (H)C(CO)NH-TOCSY experiment is presented for the sequential assignment of the protonated methyl groups. A high-sensitivity spectrum is recorded on a 15N, 13C, 2H, 1H3C-labeled SH2 domain at 3°C (correlation time 18.8 ns), demonstrating the utility of the method for proteins in the 30–40 kDa molecular weight range.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00410333
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  • 4
    Electronic Resource
    Electronic Resource
    Effect of oxygen removal on hydrogen photoproduction in algae (1983)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 25 (1983), S. 1897-1904 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Hydrogen photoproduction from water in Scenedesmus cells requires removal of oxygen by a reagent in contact with the algae. Both deoxyhemoglobin and deoxymyoglobin stimulated hydrogen production by reversible absorption of oxygen. Their effectiveness was greatly increased when other oxygen-combining reagents were present in a separate chamber with deoxyhemoglobin and deoxymyoglobin serving as reversible oxygen transfer agents.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260250716
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