1H NMR Spectrum

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Lorenza Trabalzini - One of the best experts on this subject based on the ideXlab platform.

  • inferences on the nature of a cr v or cr iv species formed by reduction of dichromate by a bovine liver homogenate NMR and mass spectrometric studies
    Bioinorganic Chemistry and Applications, 2003
    Co-Authors: Elena Gaggelli, Nicola Damelio, Nicola Gaggelli, Gianni Valensin, Lucia Bovalini, Alessandro Paffetti, Lorenza Trabalzini
    Abstract:

    A low-molecular weight chromium-containing fraction of the material resulting from dichromate reduction by bovine liver homogenate was investigated by NMR and ES-MS. The ES-MS Spectrum showed a readily detectable peak at m/z = 786.1. The same molecular weight reasonably agreed with the relatively low diffusion coefficient measured by NMR-DOSY experiments on the main species observed in the 1H NMR Spectrum. At least two downfield shifted and broad paramagnetic signals were apparent in the 1H NMR Spectrum. Temperature dependence of chemical shift was exploited in order to estimate the diamagnetic shift of the signals in the diamagnetic region of the Spectrum. 2D TOCSY, NOESY, COSY and 1H-3C HMQC spectra revealed the presence of aromatic protons (which were assigned as His residues), Gly and some other short chain amino-acids. Combinations of the molecular masses of such components together with acetate (which is present in the solution) and chromium atoms allowed a tentative proposal of a model for the compound.

  • Inferences on the Nature of a Cr(V) or Cr(IV) Species Formed by Reduction of Dichromate by a Bovine Liver Homogenate: NMR and Mass-Spectrometric Studies
    Hindawi Publishing Corporation, 2003
    Co-Authors: Elena Gaggelli, Nicola Gaggelli, Gianni Valensin, Lucia Bovalini, Alessandro Paffetti, Nicola D'amelio, Lorenza Trabalzini
    Abstract:

    A low-molecular weight chromium-containing fraction of the material resulting from dichromate reduction by bovine liver homogenate was investigated by NMR and ES-MS. The ES-MS Spectrum showed a readily detectable peak at m/z = 786.1. The same molecular weight reasonably agreed with the relatively low diffusion coefficient measured by NMR-DOSY experiments on the main species observed in the 1H NMR Spectrum. At least two downfield shifted and broad paramagnetic signals were apparent in the 1H NMR Spectrum. Temperature dependence of chemical shift was exploited in order to estimate the diamagnetic shift of the signals in the diamagnetic region of the Spectrum. 2D TOCSY, NOESY, COSY and 1H-3C HMQC spectra revealed the presence of aromatic protons (which were assigned as His residues), Gly and some other short chain amino-acids. Combinations of the molecular masses of such components together with acetate (which is present in the solution) and chromium atoms allowed a tentative proposal of a model for the compound

C W Hilbers - One of the best experts on this subject based on the ideXlab platform.

  • assignment of the 1H NMR Spectrum and secondary structure elucidation of the single stranded dna binding protein encoded by the filamentous bacteriophage ike
    Biochemistry, 1992
    Co-Authors: J P M Van Duynhoven, Ruud N.h. Konings, Paul J M Folkers, C W J M Prinse, B J M Harmsen, C W Hilbers
    Abstract:

    By means of 2D NMR techniques, all backbone resonances in the 1H NMR Spectrum of the single-stranded DNA binding protein encoded by gene V of the filamentous phage IKe have been assigned sequence specifically (at pH 4.6, T = 298 K). In addition, a major part of the side chain resonances could be assigned as well. Analysis of NOESY data permitted the elucidation of the secondary structure of IKe gene V protein. The major part of this secondary structure is present as an antiparallel beta-sheet, i.e., as two beta-loops which partly combine into a triple-stranded beta-sheet structure, one beta-loop and one triple-stranded beta-sheet structure. It is shown that a high degree of homology exists with the secondary structure of the single-stranded DNA binding protein encoded by gene V of the distantly related filamentous phage M13.

  • assignment of the 600 mhz 1H NMR Spectrum of amicyanin from thiobacillus versutus by two dimensional NMR methods provides information on secondary structure
    FEBS Journal, 1991
    Co-Authors: Arjen Lommen, C W Hilbers, Sybren S Wijmenga, Gerard W Canters
    Abstract:

    The nearly complete assignment (pH6.8; T310 K) of the 1H-NMR Spectrum of reduced amicyanin from Thiobacillus versutus is reported. Experimental evidence is presented, that the structure of the amicyanin contains two β-sheets, a feature common to plastocyanins and azurins. The loops joining the β-strands have also been identified. The loop F-G (Thr94–Phe98), together with the flanking residues Cys93 and Met99, comprises three of the four copper ligandes and is short compared to similar loops in plastocyanin and azurin. His96 turns out to be the copper ligand that can be protonated. Amicyanin resembles plastocyanin in overall structure but differs from it on account of an N-terminal strand of 22 amino acids in front of strand A, shorter loops A-B, D-E and F-G and the absence of any α-helical segments.

Gordon C K Roberts - One of the best experts on this subject based on the ideXlab platform.

  • sequence specific resonance assignment and conformational analysis of subtilin by 2d NMR
    FEBS Letters, 1992
    Co-Authors: Weng C Chan, Barrie W Bycroft, Mark L Leyland, Luyun Lian, Jichun Yang, Gordon C K Roberts
    Abstract:

    Subtilin, a 32-amino acid peptide with potent antimicrobial activity, has been isolated from Bacillus subtilis ATCC6633. The chemical structure has been confirmed by the unambiguous sequence-specific assignment of its 1H NMR Spectrum. Detailed NMR analysis revealed that subtilin is a rather flexible molecule; the only observed conformational contraints were those imposed by the cyclic structures created by the tanthionine and 3-methyllanthionine residues. These results suggest that in aqueous solution subtilin and the homologous peptide nisin have similar conformation.

Elena Gaggelli - One of the best experts on this subject based on the ideXlab platform.

  • inferences on the nature of a cr v or cr iv species formed by reduction of dichromate by a bovine liver homogenate NMR and mass spectrometric studies
    Bioinorganic Chemistry and Applications, 2003
    Co-Authors: Elena Gaggelli, Nicola Damelio, Nicola Gaggelli, Gianni Valensin, Lucia Bovalini, Alessandro Paffetti, Lorenza Trabalzini
    Abstract:

    A low-molecular weight chromium-containing fraction of the material resulting from dichromate reduction by bovine liver homogenate was investigated by NMR and ES-MS. The ES-MS Spectrum showed a readily detectable peak at m/z = 786.1. The same molecular weight reasonably agreed with the relatively low diffusion coefficient measured by NMR-DOSY experiments on the main species observed in the 1H NMR Spectrum. At least two downfield shifted and broad paramagnetic signals were apparent in the 1H NMR Spectrum. Temperature dependence of chemical shift was exploited in order to estimate the diamagnetic shift of the signals in the diamagnetic region of the Spectrum. 2D TOCSY, NOESY, COSY and 1H-3C HMQC spectra revealed the presence of aromatic protons (which were assigned as His residues), Gly and some other short chain amino-acids. Combinations of the molecular masses of such components together with acetate (which is present in the solution) and chromium atoms allowed a tentative proposal of a model for the compound.

  • Inferences on the Nature of a Cr(V) or Cr(IV) Species Formed by Reduction of Dichromate by a Bovine Liver Homogenate: NMR and Mass-Spectrometric Studies
    Hindawi Publishing Corporation, 2003
    Co-Authors: Elena Gaggelli, Nicola Gaggelli, Gianni Valensin, Lucia Bovalini, Alessandro Paffetti, Nicola D'amelio, Lorenza Trabalzini
    Abstract:

    A low-molecular weight chromium-containing fraction of the material resulting from dichromate reduction by bovine liver homogenate was investigated by NMR and ES-MS. The ES-MS Spectrum showed a readily detectable peak at m/z = 786.1. The same molecular weight reasonably agreed with the relatively low diffusion coefficient measured by NMR-DOSY experiments on the main species observed in the 1H NMR Spectrum. At least two downfield shifted and broad paramagnetic signals were apparent in the 1H NMR Spectrum. Temperature dependence of chemical shift was exploited in order to estimate the diamagnetic shift of the signals in the diamagnetic region of the Spectrum. 2D TOCSY, NOESY, COSY and 1H-3C HMQC spectra revealed the presence of aromatic protons (which were assigned as His residues), Gly and some other short chain amino-acids. Combinations of the molecular masses of such components together with acetate (which is present in the solution) and chromium atoms allowed a tentative proposal of a model for the compound

Takakazu Yamamoto - One of the best experts on this subject based on the ideXlab platform.

  • The First Observation of 1H-NMR Spectrum of Pentacene
    Japanese Journal of Applied Physics, 2004
    Co-Authors: Mika Nagano, Hiroki Fukumoto, Tetsuya Hasegawa, Norikatsu Myoujin, Jun Yamaguchi, Takakazu Yamamoto, Kenji Itaka, Hideomi Koinuma
    Abstract:

    Despite much interest in pentacene as a promising organic semiconductors, its chemical properties have scarcely been elucidated. Even such a fundamental data as 1H-NMR Spectrum has not been reported yet due to poor solubility of pentacene in various solvents. Here we report the first observation of 1H NMR Spectrum of pentacene by using dimethyl sulfoxide-d6 as solvent and heating the sample to 80°C. Not only the signal assignment but also the easily oxidizable property of pentacene was verified from the comparison between the spectra measured in degassed and non-degassed solvents.

  • A Novel Crown Ether Stopping Group for Side Chain Polyrotaxane. Preparation of Side Chain Polybenzimidazole Rotaxane Containing Alkyl Side Chain Ended by Crown Ether−ONa Group
    Macromolecules, 2000
    Co-Authors: Isao Yamaguchi, Kohtaro Osakada, Takakazu Yamamoto
    Abstract:

    NaH promoted deprotonation of the NH group in poly(p-phenylenebenzimidazole) (1) followed by treatment with Br(CH2)12OH causes substitution of the NH hydrogen of 1 to give N-alkylated polymer (2) having a −CH2ONa group at the end of the side chain. The 1H NMR Spectrum of 2 indicates that 90% of the imidazole rings are N-alkylated. Stirring a DMF solution of 2 with α-cyclodextrin (α-CD) leads to inclusion of α-CD onto the N-alkyl side chain, and subsequent addition of 15-crown 5-ether (15C5) causes complex formation of the −ONa group with 15C5. Because of the formation of the bulky 15C5−ONa end group, dethreading of α-CD from the side chain is prevented. The 1H NMR Spectrum of the side chain polyrotaxane (4) reveals that α-CD is incorporated in 57% of the side chain and that all the ONa groups form the complex with 15C5. GPC and DSC profiles of 4 support formation of the side chain polyrotaxane. Treatment of 4 with H2O causes detaching of 15C5 and dethreading of α-CD from the side chain.