The use of TROSY for detection and suppression of conformational exchange NMR line broadening in biological macromolecules.

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：: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：:Fast multidimensional NMR with a time resolution of a few seconds provides a new tool for high throughput screening and site-resolved real-time studies of kinetic molecular processes by NMR. Recently we have demonstrated the feasibility to record protein 1H-15N correlation spectra in a few seconds of acquisition time ...

journal_title：Journal of biomolecular NMR

authors： Schanda P,Kupce E,Brutscher B

更新日期：2005-12-01 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：:In our previous work, we proposed a new way to represent protein native states, using ensembles of a small number of conformations with relative Populations, or ESP in short. Using Ubiquitin as an example, we showed that using a small number of conformations could greatly reduce the potential of overfitting and assign...

journal_title：Journal of biomolecular NMR

authors： Vammi V,Song G

更新日期：2015-12-01 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：:The transmembrane protein YuaF from B. subtilis is a member of the NfeD-like clan with a potential role in maintaining membrane integrity during conditions of cellular stress. nfeD-genes are primarily found in highly conserved operon structures together with the gene of another membrane protein belonging to the SPFH s...

journal_title：Journal of biomolecular NMR

authors： Walker CA,Hinderhofer M,Witte DJ,Boos W,Möller HM

更新日期：2008-09-01 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：:New methods are described for accurate measurement of multiple residual dipolar couplings in nucleic acid bases. The methods use TROSY-type pulse sequences for optimizing resolution and sensitivity, and rely on the E.COSY principle to measure the relatively small two-bond (2)D(CH) couplings at high precision. Measurem...

journal_title：Journal of biomolecular NMR

authors： Boisbouvier J,Bryce DL,O'neil-Cabello E,Nikonowicz EP,Bax A

更新日期：2004-11-01 00:00:00

abstract：:We propose a method for the determination of (15)N csa/dipolar cross-correlation rates based on the measurement of the two apparent transverse (or longitudinal) relaxation rates associated with each component of the nitrogen doublet (N(alpha) and N(beta)). This is achieved by inserting a spin state selective scheme in...

journal_title：Journal of biomolecular NMR

authors： Bouguet-Bonnet S,Mutzenhardt P,Canet D

更新日期：2004-10-01 00:00:00

abstract：:The question is addressed of how maximal structural NOE data on double labelled proteins can be acquired with a minimal set of NOESY experiments. Two 3D-NOESY spectra are reported which, in concert with other commonly used spectra, provide a convenient strategy for NOE assignment. The 3D CNH-NOESY and 3D NCH-NOESY pro...

journal_title：Journal of biomolecular NMR

authors： Diercks T,Coles M,Kessler H

更新日期：1999-10-01 00:00:00

abstract：:Glycoproteins are characterized by the heterogeneous and dynamic nature of their glycan moieties, which hamper crystallographic analysis. NMR spectroscopy provides potential advantages in dealing with such complicated systems, given that the target molecules can be isotopically labeled. Methods of metabolic isotope la...

journal_title：Journal of biomolecular NMR

authors： Yanaka S,Yagi H,Yogo R,Yagi-Utsumi M,Kato K

更新日期：2018-07-01 00:00:00

abstract：:The binding site and backbone dynamics of a bioactive complex formed by the acidic fibroblast growth factor (FGF-1) and a specifically designed heparin hexasaccharide has been investigated by HSQC and relaxation NMR methods. The comparison of the relaxation data for the free and bound states has allowed showing that t...

journal_title：Journal of biomolecular NMR

authors： Canales-Mayordomo A,Fayos R,Angulo J,Ojeda R,Martín-Pastor M,Nieto PM,Martín-Lomas M,Lozano R,Giménez-Gallego G,Jiménez-Barbero J

更新日期：2006-08-01 00:00:00

abstract：:We discuss the optimum experimental conditions to obtain assignment spectra for solid proteins at magic-angle spinning (MAS) frequencies around 100 kHz. We present a systematic examination of the MAS dependence of the amide proton T 2' times and a site-specific comparison of T 2' at 93 kHz versus 60 kHz MAS frequency....

journal_title：Journal of biomolecular NMR

authors： Penzel S,Smith AA,Agarwal V,Hunkeler A,Org ML,Samoson A,Böckmann A,Ernst M,Meier BH

更新日期：2015-10-01 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：:NMR of macromolecules is limited by large transverse relaxation rates. In practice, this results in low efficiency of coherence transfer steps in multidimensional NMR experiments, leading to poor sensitivity and long acquisition times. The efficiency of coherence transfer can be maximized by design of relaxation optim...

journal_title：Journal of biomolecular NMR

authors： Frueh DP,Ito T,Li JS,Wagner G,Glaser SJ,Khaneja N

更新日期：2005-05-01 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：:Simultaneous recording of different NMR parameters is an efficient way to reduce the overall experimental time and speed up structural studies of biological macromolecules. This can especially be beneficial in the case of fast NMR-based drug screening applications or for collecting NOE restraints, where prohibitively ...

journal_title：Journal of biomolecular NMR

authors： Würtz P,Aitio O,Hellman M,Permi P

更新日期：2007-10-01 00:00:00

abstract：:Limitations in the applicability, accuracy, and precision of individual structure characterization methods can sometimes be overcome via an integrative modeling approach that relies on information from all available sources, including all available experimental data and prior models. The open-source Integrative Modeli...

journal_title：Journal of biomolecular NMR

authors： Vallat B,Webb B,Westbrook J,Sali A,Berman HM

更新日期：2019-07-01 00:00:00

abstract：:A computer program has been developed to accurately and automatically predict the 1H and 13C chemical shifts of unassigned proteins on the basis of sequence homology. The program (called SHIFTY) uses standard sequence alignment techniques to compare the sequence of an unassigned protein against the BioMagResBank--a pu...

journal_title：Journal of biomolecular NMR

authors： Wishart DS,Watson MS,Boyko RF,Sykes BD

更新日期：1997-12-01 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：: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：:The NMR spectra of the complex between the DNA-binding domain of the Dead ringer protein (DRI-DBD, Gly262-Gly398) and its DNA binding site (DRI-DBD:DNA, 26 kDa) have been optimized by biochemical and spectroscopic means. First, we demonstrate the utility of a modified 2D [F1,F2] 13C-filtered NOESY experiment that empl...

journal_title：Journal of biomolecular NMR

authors： Iwahara J,Wojciak JM,Clubb RT

更新日期：2001-03-01 00:00:00

abstract：:Three experiments are introduced to determine a complete set of coupling constants in RNA oligomers. In the HCCH-E.COSY experiment, the vicinal proton-proton coupling constants can be measured with high accuracy. In the P-FIDS-CT-HSQC experiment, vicinal proton-phosphorus and carbon-phosphorus couplings are measured t...

journal_title：Journal of biomolecular NMR

authors： Schwalbe H,Marino JP,King GC,Wechselberger R,Bermel W,Griesinger C

更新日期：1994-09-01 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 arrival of very high field magnets and cryogenic circuitries, and the development of relaxation-optimized pulse sequences have added powerful tools for increasing sensitivity and resolution in NMR studies of biomacromolecules. The potential of these advances is not fully realized in practice, however, since curren...

journal_title：Journal of biomolecular NMR

authors： Rovnyak D,Hoch JC,Stern AS,Wagner G

更新日期：2004-09-01 00:00:00

abstract：:Under the condition that the longitudinal relaxation time of spin I is shorter than the longitudinal relaxation time of spin S the steady-state magnetization in [S,I]-TROSY-type experiments can be enhanced by intermediate storage of a part of the steady-state magnetization of spin I on spin S with a pulse sequence ele...

journal_title：Journal of biomolecular NMR

authors： Riek R

更新日期：2001-10-01 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：:Protein-nucleic acid interactions involve intermolecular ion pairs of protein side-chain and DNA or RNA phosphate groups. Using three protein-DNA complexes, we demonstrate that site-specific oxygen-to-sulfur substitution in phosphate groups allows for identification of NMR signals from the protein side-chain NH3 (+) g...

journal_title：Journal of biomolecular NMR

authors： Anderson KM,Nguyen D,Esadze A,Zandrashvili L,Gorenstein DG,Iwahara J

更新日期：2015-05-01 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