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

abstract：:Sparse sampling in biomolecular multidimensional NMR offers increased acquisition speed and resolution and, if appropriate conditions are met, an increase in sensitivity. Sparse sampling of indirectly detected time domains combined with the direct truly multidimensional Fourier transform has elicited particular attent...

journal_title：Journal of biomolecular NMR

authors： Gledhill JM Jr,Wand AJ

更新日期：2012-01-01 00:00:00

abstract：:Understanding of the molecular mechanisms of protein function requires detailed insight into the conformational landscape accessible to the protein. Conformational changes can be crucial for biological processes, such as ligand binding, protein folding, and catalysis. NMR spectroscopy is exquisitely sensitive to such ...

journal_title：Journal of biomolecular NMR

authors： Chatterjee SD,Ubbink M,van Ingen H

更新日期：2018-06-01 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：:Strong solvent signals lead to a disappearance of weak protein signals close to the solvent resonance frequency and to base plane variations all over the spectrum. AUREMOL-SSA provides an automated approach for solvent artifact removal from multidimensional NMR protein spectra. Its core algorithm is based on singular ...

journal_title：Journal of biomolecular NMR

authors： Malloni WM,De Sanctis S,Tomé AM,Lang EW,Munte CE,Neidig KP,Kalbitzer HR

更新日期：2010-06-01 00:00:00

abstract：:We present heteronuclear three-dimensional gradient-NMR techniques for the resonanceassignment of exchangeable (-OH and -NH) protons in uniformly 13C isotopically enrichedoligosaccharides and for the measurement of 1H-1H nuclear Overhauser enhancementsinvolving these protons. These techniques are derived from conventi...

journal_title：Journal of biomolecular NMR

authors： Harris R,Rutherford TJ,Milton MJ,Homans SW

更新日期：1997-01-01 00:00:00

abstract：:This paper presents new methods designed for quantitative analysis of chemical shift perturbation NMR spectra. The methods automatically trace the displacements of cross peaks between a perturbed test spectrum and the reference spectrum (or among a series of titration spectra), and measure the changes of chemical shif...

journal_title：Journal of biomolecular NMR

authors： Peng C,Unger SW,Filipp FV,Sattler M,Szalma S

更新日期：2004-08-01 00:00:00

abstract：:No matter the source of compounds, drug discovery campaigns focused directly on the target are entirely dependent on a consistent stream of reliable data that reports on how a putative ligand interacts with the protein of interest. The data will derive from many sources including enzyme assays and many types of biophy...

journal_title：Journal of biomolecular NMR

authors： Keiffer S,Carneiro MG,Hollander J,Kobayashi M,Pogoryelev D,Ab E,Theisgen S,Müller G,Siegal G

更新日期：2020-11-01 00:00:00

abstract：:This paper describes the use of single transition-to-single transition polarization transfer (ST2-PT) in transverse relaxation-optimized spectroscopy (TROSY), where it affords a [Formula: see text] sensitivity enhancement for kinetically stable amide 15N-1H groups in proteins. Additional, conventional improvements of ...

journal_title：Journal of biomolecular NMR

authors： Pervushin KV,Wider G,Wüthrich K

更新日期：1998-08-01 00:00:00

abstract：:Spectral densities of the 15N amide in Escherichia coli ribonuclease HI, obtained from NMR relaxation experiments, were compared with those calculated using a molecular dynamics (MD) simulation. All calculations and comparisons assumed that the auto-correlation function describing the internal motions of the molecule ...

journal_title：Journal of biomolecular NMR

authors： Ishima R,Yamasaki K,Saito M,Nagayama K

更新日期：1995-09-01 00:00:00

abstract：:The importance of protein chemical shift values for the determination of three-dimensional protein structure has increased in recent years because of the large databases of protein structures with assigned chemical shift data. These databases have allowed the investigation of the quantitative relationship between chem...

journal_title：Journal of biomolecular NMR

authors： Meiler J

更新日期：2003-05-01 00:00:00

abstract：:We report the determination of the global fold of human ubiquitin using protein backbone NMR residual dipolar coupling and long-range nuclear Overhauser effect (NOE) data as conformational restraints. Specifically, by use of a maximum of three backbone residual dipolar couplings per residue (Ni-H N i, Ni-C'(i-1), H N ...

journal_title：Journal of biomolecular NMR

authors： Giesen AW,Homans SW,Brown JM

更新日期：2003-01-01 00:00:00

abstract：:Proton chemical shifts of a series of disordered linear peptides (H-Gly-Gly-X-Gly-Gly-OH, with X being one of the 20 naturally occurring amino acids) have been obtained using 1D and 2D 1H NMR at pH 5.0 as a function of temperature and solvent composition. The use of 2D methods has allowed some ambiguities in side-chai...

journal_title：Journal of biomolecular NMR

authors： Merutka G,Dyson HJ,Wright PE

更新日期：1995-01-01 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：: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：:The kinetics of lanthanide (III) exchange for calcium(II) in the C-terminal EF-hand of the protein calbindin D9k have been studied by one-dimensional (1D) stopped-flow NMR. By choosing a paramagnetic lanthanide (Ce3+), kinetics in the sub-second range can be easily measured. This is made possible by the fact that (i) ...

journal_title：Journal of biomolecular NMR

authors： Barbieri R,Hore PJ,Luchina C,Pierattelli R

更新日期：2002-08-01 00:00:00

abstract：:G protein-coupled receptors (GPCRs) are transmembrane signal transducers which regulate many key physiological process. Since their discovery, their analysis has been limited by difficulties in obtaining sufficient amounts of the receptors in high-quality, functional form from heterologous expression hosts. Albeit hig...

journal_title：Journal of biomolecular NMR

authors： Abiko LA,Rogowski M,Gautier A,Schertler G,Grzesiek S

更新日期：2021-01-27 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：:Signal overlapping is a major bottleneck for protein NMR analysis. We propose a new method, stable-isotope-assisted parameter extraction (SiPex), to resolve overlapping signals by a combination of amino-acid selective isotope labeling (AASIL) and tensor decomposition. The basic idea of Sipex is that overlapping signal...

journal_title：Journal of biomolecular NMR

authors： Kasai T,Ono S,Koshiba S,Yamamoto M,Tanaka T,Ikeda S,Kigawa T

更新日期：2020-03-01 00:00:00

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

authors： Petros AM,Neri P,Fesik SW

更新日期：1992-01-01 00:00:00

abstract：:The (1)H, (13)C and (15)N NMR resonances of the backbone of serine protease PB92 have been assigned. This 269-residue protein is one of the largest monomeric proteins assigned so far. The amount and quality of information available suggest that even larger proteins could be assigned with present methods. Measured chem...

journal_title：Journal of biomolecular NMR

authors： Fogh RH,Schipper D,Boelens R,Kaptein R

更新日期：1994-01-01 00:00:00

abstract：:We present and test two methods to use quantum chemical calculations to improve standard protein structure refinement by molecular dynamics simulations restrained to experimental NMR data. In the first, we replace the molecular mechanics force field (employed in standard refinement to supplement experimental data) for...

journal_title：Journal of biomolecular NMR

authors： Hsiao YW,Drakenberg T,Ryde U

更新日期：2005-02-01 00:00:00

abstract：:We perform a detailed comparison of fast backbone dynamics probed at amide nitrogen versus carbonyl carbon sites for dematin headpiece C-terminal domain (DHP) and its S74E mutant (DHPS74E). Carbonyl dynamics is probed via auto-correlated longitudinal rates and transverse C'/C'-C(alpha) CSA/dipolar and C'/C'-N CSA/dipo...

journal_title：Journal of biomolecular NMR

authors： Vugmeyster L,Ostrovsky D,Li Y

更新日期：2010-06-01 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：:Considerable excitement has been aroused by recent new methods for speeding up multidimensional NMR experiments by radically modifying the normal time-domain sampling protocols. These new schemes include the filter diagonalization method, GFT-NMR, the single-scan two-dimensional technique, Hadamard spectroscopy, and a...

journal_title：Journal of biomolecular NMR

authors： Freeman R,Kupce E

更新日期：2003-10-01 00:00:00

abstract：:Four novel amino acid type-selective triple resonance experiments to identify the backbone amino proton and nitrogen resonances of Arg and Lys and of their sequential neighbors in (13C,15N)-labeled proteins are presented: the R(i+1)-HSQC and R(i,i+1)-HSQC select signals originating from Arg side chains, the K(i+1)-HSQ...

journal_title：Journal of biomolecular NMR

authors： Schubert M,Oschkinat H,Schmieder P

更新日期：2001-08-01 00:00:00

abstract：:Methyl (13)CHD(2) isotopomers of all methyl-containing amino-acids can be observed in residually protonated samples of large proteins obtained from [U-(13)C,(1)H]-glucose/D(2)O-based bacterial media, with sensitivity sufficient for a number of NMR applications. Selective detection of some subsets of methyl groups (Ala...

journal_title：Journal of biomolecular NMR

authors： Guo C,Tugarinov V

更新日期：2010-02-01 00:00:00

abstract：:In magic angle spinning solid state NMR experiments the potential of heteronuclear (1)H decoupling employing a continuous train of adiabatic inversion pulses has been assessed via numerical simulations and experimental measurements. It is shown that, with a (1)H RF field strength of approximately 100 kHz that is typic...

journal_title：Journal of biomolecular NMR

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

更新日期：2004-07-01 00:00:00

abstract：:NifU-like proteins are a highly conserved protein that serves as the scaffold for assembly of Fe-S clusters. Chloroplastic NifU-like proteins have tandem NifU like domains, named domain I and domain II. Although the amino acid sequences of these domains are very similar to each other, the predicted functional region f...

journal_title：Journal of biomolecular NMR

authors： Kumeta H,Ogura K,Asayama M,Katoh S,Katoh E,Teshima K,Inagaki F

更新日期：2007-06-01 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：:The solution structure of the SH3 domain of human p56 Lck tyrosine kinase (Lck-SH3) has been determined by multidimensional heteronuclear NMR spectroscopy. The structure was calculated from a total of 935 experimental restraints comprising 785 distance restraints derived from 1017 assigned NOE cross peaks and 150 dihe...

journal_title：Journal of biomolecular NMR

authors： Hiroaki H,Klaus W,Senn H

更新日期：1996-09-01 00:00:00