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  • Conformational analysis of alpha-D-Fuc-(1-->4)-beta-D-GlcNAc-OMe. One-dimensional transient NOE experiments and Metropolis Monte Carlo simulations.

    abstract::One-dimensional transient NOE build-up curves were measured for the synthetic disaccharide alpha-D-Fuc-(1-->4)-beta-D-GlcNAc 1 utilizing Gaussian shaped pulses. Simulated build-up curves from Metropolis Monte Carlo simulations were compared to the experimental data. Disaccharide 1 is structurally related to methyl bet...

    journal_title:Journal of biomolecular NMR

    pub_type: 杂志文章

    doi:10.1007/BF00176007

    authors: Weimar T,Meyer B,Peters T

    更新日期:1993-07-01 00:00:00

  • Proton, carbon, and nitrogen chemical shifts accurately delineate differences and similarities in secondary structure between the homologous proteins IRAP and IL-1 beta.

    abstract::1H alpha, 13C alpha, and 15N alpha secondary shifts, defined as the difference between the observed value and the random coil value, have been calculated for interleukin-1 receptor antagonist protein and interleukin-1 beta. Averaging of the secondary chemical shifts with those of adjacent residues was used to smooth o...

    journal_title:Journal of biomolecular NMR

    pub_type: 杂志文章

    doi:10.1007/BF02192848

    authors: Stockman BJ,Scahill TA,Strakalaitis NA,Brunner DP,Yem AW,Deibel MR Jr

    更新日期:1992-11-01 00:00:00

  • Structure and conformation in solution of the parallel-stranded hybrid alpha-d(CGCAATTCGC).beta-d(GCGTTAAGCG) by high-resolution 2D NMR.

    abstract::The unnatural duplex oligonucleotide alpha-d(CGCAATTCGC).beta-d(GCGTTAAGCG) was analyzed by high-resolution NMR methods. All of the exchangeable imino and nonexchangeable protons of the duplex were assigned. Detection of all 10 of the exchangeable imino protons confirms that a parallel, unsymmetrical duplex is formed....

    journal_title:Journal of biomolecular NMR

    pub_type: 杂志文章

    doi:10.1007/BF01875321

    authors: Gmeiner WH,Rayner B,Morvan F,Imbach JL,Lown JW

    更新日期:1992-05-01 00:00:00

  • 1H NMR studies of deuterated ribonuclease HI selectively labeled with protonated amino acids.

    abstract::Two-dimensional (2D) 1H NMR experiments using deuterium labeling have been carried out to investigate the solution of ribonuclease HI (RNase HI) from Escherichia coli (E. coli), which consists of 155 amino acids. To simplify the 1H NMR spectra, two fully deuterated enzymes bearing several protonated amino acids were p...

    journal_title:Journal of biomolecular NMR

    pub_type: 杂志文章

    doi:10.1007/BF01875525

    authors: Oda Y,Nakamura H,Yamazaki T,Nagayama K,Yoshida M,Kanaya S,Ikehara M

    更新日期:1992-03-01 00:00:00

  • Sequence-specific resonance assignment and secondary structure of (1-71) bacterioopsin.

    abstract::The conformation of chymotryptic fragment C2 of bacteriohodopsin (residues 1-71) was studied by 2D 1H NMR. The fragment was solubilized in a mixture of chloroform/methanol (1:1), 0.1 M LiClO4. Most of the resonances in 1H NMR spectra of fragment C2 were assigned using phase-sensitive DQF-COSY, TOCSY, and NOESY techniq...

    journal_title:Journal of biomolecular NMR

    pub_type: 杂志文章

    doi:10.1007/BF01875527

    authors: Sobol AG,Arseniev AS,Abdulaeva GV,Musina LYu,Bystrov VF

    更新日期:1992-03-01 00:00:00

  • Identification of solvent-exposed regions of an FK-506 analog, ascomycin, bound to FKBP using a paramagnetic probe.

    abstract::The solvent-exposed regions of (U-13C)ascomycin when bound to its putative target protein, FKBP, have been identified based on the different proton longitudinal relaxation rates (R1 = 1/T1) measured in the absence and presence of the paramagnetic relaxation reagent, 4-hydroxy-2,2,6,6-tetramethyl-piperidinyl-1-oxy (HyT...

    journal_title:Journal of biomolecular NMR

    pub_type: 杂志文章

    doi:10.1007/BF02192797

    authors: Petros AM,Neri P,Fesik SW

    更新日期:1992-01-01 00:00:00

  • Measurement of 15N-13C J couplings in staphylococcal nuclease.

    abstract::15N-C alpha and 15N-C' J couplings were measured for the backbone of staphylococcal nuclease, uniformly enriched with 15N and 13C. It is found that the 1JC'N coupling is similar for beta-sheet, J = 14.8 +/- 0.5 and for alpha-helix, J = 14.8 +/- 0.4 but tends to be larger for the unstructured N- and C-terminal ends of ...

    journal_title:Journal of biomolecular NMR

    pub_type: 杂志文章

    doi:10.1007/BF02192865

    authors: Delaglio F,Torchia DA,Bax A

    更新日期:1991-11-01 00:00:00

  • Improved three-dimensional 1H-13C-1H correlation spectroscopy of a 13C-labeled protein using constant-time evolution.

    abstract::An improved version of the three-dimensional HCCH-COSY NMR experiment is described that correlates the resonances of geminal and vicinal proton pairs with the chemical shift of the 13C nucleus attached to one of the protons. The experiment uses constant-time evolution of transverse 13C magnetization which optimizes tr...

    journal_title:Journal of biomolecular NMR

    pub_type: 杂志文章

    doi:10.1007/BF01875522

    authors: Ikura M,Kay LE,Bax A

    更新日期:1991-09-01 00:00:00

  • Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cytochrome c2: a 1H-15N NMR study.

    abstract::The hydrogen-deuterium exchange rates of the reduced and oxidized forms of Rhodobacter capsulatus cytochrome c2 were studied by 1H-15N homonuclear multiple quantum correlation spectroscopy. Minimal differences were observed for the N- and C-terminal helices on changing redox state suggesting that although these helice...

    journal_title:Journal of biomolecular NMR

    pub_type: 杂志文章

    doi:10.1007/BF01877226

    authors: Gooley PR,Zhao D,MacKenzie NE

    更新日期:1991-07-01 00:00:00

  • Efficient analysis of protein 2D NMR spectra using the software package EASY.

    abstract::The program EASY supports the spectral analysis of biomacromolecular two-dimensional (2D) nuclear magnetic resonance (NMR) data. It provides a user-friendly, window-based environment in which to view spectra for interactive interpretation. In addition, it includes a number of automated routines for peak-picking, spin-...

    journal_title:Journal of biomolecular NMR

    pub_type: 杂志文章

    doi:10.1007/BF01877224

    authors: Eccles C,Güntert P,Billeter M,Wüthrich K

    更新日期:1991-07-01 00:00:00

  • Temperature-jump NMR study of protein folding: ribonuclease A at low pH.

    abstract::The kinetic process of folding of bovine pancreatic ribonuclease A in a 2H2O environment at pH 1.2 was examined by a recently developed temperature-jump NMR method (Akasaka et al., (1990) Rev. Sci. Instrum. 61, 66-68). Upon temperature-jump down from 45 degrees C to 29 degrees C, which was attained within 6 s, the pro...

    journal_title:Journal of biomolecular NMR

    pub_type: 杂志文章

    doi:10.1007/BF01874569

    authors: Akasaka K,Naito A,Nakatani H

    更新日期:1991-05-01 00:00:00

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