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

abstract：:Protein structure determination by NMR methods has started in the mid-eighties and has been growing steadily since then. Ca. 14% of the protein structures deposited in the PDB have been solved by NMR. The evaluation of the quality of NMR structures however is still lacking a well-established practice. In this work, we...

journal_title：Journal of biomolecular NMR

authors： Saccenti E,Rosato A

更新日期：2008-04-01 00:00:00

abstract：:We present NMRlib, a suite of jython-based tools designed for Bruker spectrometers (TopSpin versions 3.2-4.0) that allow easy setup, management, and exchange of NMR experiments. A NMR experiment can be set up and executed in a few clicks by navigating through the NMRlib GUI tree structure, without any further paramete...

journal_title：Journal of biomolecular NMR

authors： Favier A,Brutscher B

更新日期：2019-05-01 00:00:00

abstract：:A substantial time savings in the collection of multidimensional NMR data can be achieved by coupling the evolution of nuclei in the indirect dimensions. In order to save time, the sampling of the indirect dimensions is inherently incomplete. Therefore, many algorithms and samplings schemes have been developed aimed a...

journal_title：Journal of biomolecular NMR

authors： Mueller GA

更新日期：2009-05-01 00:00:00

abstract：:A MAS solid state NMR approach for achieving efficient scalar coupling mediated through-bond (13)C chemical shift correlations of the aliphatic carbons in uniformly labelled peptides/proteins is described. The method involves the application of a continuous train of adiabatic inversion pulses, as in the adiabatic TOCS...

journal_title：Journal of biomolecular NMR

authors： Leppert J,Ohlenschläger O,Görlach M,Ramachandran R

更新日期：2004-06-01 00:00:00

abstract：:Simple pulse schemes are presented for the measurement of methyl (13)C and (1)H CSA values from (1)H-(13)C dipole/(13)C CSA and (1)H-(13)C dipole/(1)H CSA cross-correlated relaxation. The methodology is applied to protein L and malate synthase G. Average (13)C CSA values are considerably smaller for Ile than Leu/Val (...

journal_title：Journal of biomolecular NMR

authors： Tugarinov V,Scheurer C,Brüschweiler R,Kay LE

更新日期：2004-12-01 00:00:00

abstract：:We demonstrate a novel sparse (13)C labelling approach for methylotrophic yeast P. pastoris expression system, towards solid-state NMR studies of eukaryotic membrane proteins. The labelling scheme was achieved by co-utilizing natural abundance methanol and specifically (13)C labelled glycerol as carbon sources in the ...

journal_title：Journal of biomolecular NMR

authors： Liu J,Liu C,Fan Y,Munro RA,Ladizhansky V,Brown LS,Wang S

更新日期：2016-05-01 00:00:00

abstract：:An 'isotopomer-selected NOE' (ISNOE) method for the unequivocal identification of mutually hydrogen-bond-linked hydroxyl groups is described. It relies on the fact that the OH group's signal patterns obtained for a partially deuterated sample originate from both isotopomers of the 'partner' hydroxyl, whereas a NOE for...

journal_title：Journal of biomolecular NMR

authors： Dabrowski J,Grosskurth H,Baust C,Nifant'ev NE

更新日期：1998-07-01 00:00:00

abstract：:Selective water excitation schemes are provided which rely on the radiation damping effect in probeheads characterized by high quality factors. The schemes are implemented in homonuclear NOE and ROE experiments, designed for the selective observation of water-protein cross peaks and their assignment using standard pro...

journal_title：Journal of biomolecular NMR

authors： Otting G,Liepinsh E

更新日期：1995-06-01 00:00:00

abstract：:A three-dimensional 1H, 13C, 31P triple resonance experiment, HCP-CCH-TOCSY, is presented which provides unambiguous through-bond correlation of all 1H ribose protons on the 5' and 3' sides of the intervening phosphorus along the backbone bonding network in 13C-labeled RNA oligonucleotides. The correlation of the comp...

journal_title：Journal of biomolecular NMR

authors： Marino JP,Schwalbe H,Anklin C,Bermel W,Crothers DM,Griesinger C

更新日期：1995-01-01 00:00:00

abstract：:Protein expression in E. coli grown in shaker flasks is a routine and pivotal tool in many research laboratories. To maximize protein yields, cells are normally induced in the middle of the linear growth phase, typically at an OD600 of ≤ 1 for cells grown in Luria-Bertani (LB) medium at 37 °C. We recently showed that ...

journal_title：Journal of biomolecular NMR

authors： Cai M,Huang Y,Craigie R,Clore GM

更新日期：2019-12-01 00:00:00

abstract：:Hydroxyl protons on serine and threonine residues are not well characterized in protein structures determined by both NMR spectroscopy and X-ray crystallography. In the case of NMR spectroscopy, this is in large part because hydroxyl proton signals are usually hidden under crowded regions of (1)H-NMR spectra and remai...

journal_title：Journal of biomolecular NMR

authors： Brockerman JA,Okon M,McIntosh LP

更新日期：2014-01-01 00:00:00

abstract：:A simple triple resonance NMR experiment that leads to the correlation of the backbone amide resonances of each amino acid residue 'i' with that of residues 'i-1' and 'i+1' in ((13)C, (15)N) labelled intrinsically disordered proteins (IDPs) is presented. The experimental scheme, {HN-NCA heteronuclear TOCSY-NH}, exploi...

journal_title：Journal of biomolecular NMR

authors： Wiedemann C,Goradia N,Häfner S,Herbst C,Görlach M,Ohlenschläger O,Ramachandran R

更新日期：2015-10-01 00:00:00

abstract：:High-pressure NMR spectroscopy has emerged as a complementary approach for investigating various structural and thermodynamic properties of macromolecules. Noticeably absent from the array of experimental restraints that have been employed to characterize protein structures at high hydrostatic pressure is the residual...

journal_title：Journal of biomolecular NMR

authors： Fu Y,Wand AJ

更新日期：2013-08-01 00:00:00

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

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

abstract：:Solid-state NMR spectra of membrane proteins often show significant line broadening at cryogenic temperatures. Here we investigate the effects of several cryoprotectants to preserve the spectral resolution of lipid membranes and membrane peptides at temperatures down to ~200 K. Trehalose, glycerol, dimethylsulfoxide (...

journal_title：Journal of biomolecular NMR

authors： Lee M,Hong M

更新日期：2014-08-01 00:00:00

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

authors： Delaglio F,Torchia DA,Bax A

更新日期：1991-11-01 00:00:00

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

authors： Weimar T,Meyer B,Peters T

更新日期：1993-07-01 00:00:00

abstract：:Melittin is a naturally occurring hexacosa peptide which forms an amphiphilic helix in methanol, a random coil in water, and a tetramer of helices at basic pH or in the presence of a high salt concentration. The monomeric structure in methanol has been well characterized by proton NMR (Pastore et al. (1989) Eur. Bioph...

journal_title：Journal of biomolecular NMR

authors： Buckley P,Edison AS,Kemple MD,Prendergast FG

更新日期：1993-11-01 00:00:00

abstract：:RC-RNase is a pyrimidine-guanine sequence-specific ribonuclease and a sialic-acid-binding lectin purified from Rana catesbeiana (bullfrog) oocytes. This 111-amino acid protein exhibits cytotoxicity toward several tumor cell lines. In this paper we report the assignments of proton NMR resonances and the identification ...

journal_title：Journal of biomolecular NMR

authors： Chen C,Hom K,Huang RF,Chou PJ,Liao YD,Huang T

更新日期：1996-10-01 00:00:00

abstract：:Calmodulin is a two-domain protein which in solution can adopt a variety of conformations upon reorientation of its domains. The maximum occurrence (MO) of a set of calmodulin conformations that are representative of the overall conformational space possibly sampled by the protein, has been calculated from the paramag...

journal_title：Journal of biomolecular NMR

authors： Dasgupta S,Hu X,Keizers PH,Liu WM,Luchinat C,Nagulapalli M,Overhand M,Parigi G,Sgheri L,Ubbink M

更新日期：2011-11-01 00:00:00

abstract：:A large number of amino acids other than the canonical amino acids can now be easily incorporated in vivo into proteins at genetically encoded positions. The technology requires an orthogonal tRNA/aminoacyl-tRNA synthetase pair specific for the unnatural amino acid that is added to the media while a TAG amber or frame...

journal_title：Journal of biomolecular NMR

authors： Jones DH,Cellitti SE,Hao X,Zhang Q,Jahnz M,Summerer D,Schultz PG,Uno T,Geierstanger BH

更新日期：2010-01-01 00:00:00

abstract：:A method, based on linewidth measurements, is described which permits the rapid and facile determination of JHNH alpha coupling constants from 15N labeled proteins. Using appropriately processed HMQC-J data, we have found that a simple linear relationship exists between the half-height linewidth (delta nu1/2) of 15N-1...

journal_title：Journal of biomolecular NMR

authors： Wishart DS,Wang Y

更新日期：1998-04-01 00:00:00

abstract：:The inclusion of explicit solvent water in molecular dynamics refinement of NMR structures ought to provide the most physically meaningful accounting for the effects of solvent on structure, but is computationally expensive. In order to evaluate the validity of commonly used vacuum refinements and of recently develope...

journal_title：Journal of biomolecular NMR

authors： Xia B,Tsui V,Case DA,Dyson HJ,Wright PE

更新日期：2002-04-01 00:00:00

abstract：:During the past three years it has become possible to compute ab initio the 13C, 15N and 19F NMR chemical shifts of many sites in native proteins. Chemical shifts are beginning to become a useful supplement to more established methods of solution structure determination, and may find utility in solid-state analysis as...

journal_title：Journal of biomolecular NMR

authors： Oldfield E

更新日期：1995-04-01 00:00:00

abstract：:The systematic difference between T2 values obtained from CPMG and T1p experiments was observed for backbone 15N nuclei of bacterial ribonuclease barnase. Theoretical consideration suggests that the observed difference is caused by off-resonance effects of 180 degree pulses of the CPMG pulse train. Namely, at off-reso...

journal_title：Journal of biomolecular NMR

authors： Korzhnev DM,Tischenko EV,Arseniev AS

更新日期：2000-07-01 00:00:00

abstract：:The development of new protein labeling strategies, along with optimized experiments that exploit the label, have significantly impacted on the types of biochemical problems that can now be addressed by solution NMR spectroscopy. Here we describe how methyl labeling of key residues in a highly deuterated protein backg...

journal_title：Journal of biomolecular NMR

authors： Ruschak AM,Kay LE

更新日期：2010-01-01 00:00:00

abstract：:A new method is proposed for docking ligands into proteins in cases where an NMR-determined solution structure of a related complex is available. The method uses a set of experimentally determined values for protein-ligand, ligand-ligand, and protein-protein restraints for residues in or near to the binding site, comb...

journal_title：Journal of biomolecular NMR

authors： Polshakov VI,Morgan WD,Birdsall B,Feeney J

更新日期：1999-06-01 00:00:00

abstract：:An approach to the determination of the 2-(13)C' chemical shift (CS) tensor orientation in pyrimidine bases via heteronuclear MAS NMR spectroscopy is presented. Considering a dipolar coupled spin 1/2 network of the type S1-I-S2 consisting of directly bonded heteronuclear spins, we have carried out numerical simulation...

journal_title：Journal of biomolecular NMR

authors： Leppert J,Heise B,Ramachandran R

更新日期：2000-10-01 00:00:00

abstract：:The discovery of the TROSY effect (Pervushin et al. in Proc Natl Acad Sci USA 94:12366-12371, 1997) for reducing transverse relaxation and line sharpening through selecting pathways in which dipole-dipole and CSA Hamiltonians partially cancel each other had a tremendous impact on solution NMR studies of macromolecules...

journal_title：Journal of biomolecular NMR

authors： Takeuchi K,Arthanari H,Wagner G

更新日期：2016-12-01 00:00:00

abstract：:Structural knowledge about proteins is mainly derived from values of observables, measurable in NMR spectroscopic or X-ray diffraction experiments, i.e. absorbed or scattered intensities, through theoretically derived relationships between structural quantities such as atom positions or torsional angles on the one han...

journal_title：Journal of biomolecular NMR

authors： Steiner D,Allison JR,Eichenberger AP,van Gunsteren WF

更新日期：2012-07-01 00:00:00