S3EPY: a Sparky extension for determination of small scalar couplings from spin-state-selective excitation NMR experiments.

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：:Solid state NMR spectra from uniformly (13)C, (15)N enriched bacteriorhodospin (bR) purified from H. salinarium were acquired at 18.8 T using magic angle spinning methods. Isolated resonances of 2D (13)C-(13)C spectra exhibited 0.50-0.55 ppm line-widths. Several amino acid types could be assigned, and at least 12 out ...

journal_title：Journal of biomolecular NMR

authors： Varga K,Aslimovska L,Watts A

更新日期：2008-05-01 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：:We have developed an approach for simultaneous structure calculation and automatic Nuclear Overhauser Effect (NOE) assignment to solve nuclear magnetic resonance (NMR) structures from unassigned NOESY data. The approach, autoNOE-Rosetta, integrates Resolution Adapted Structural RECombination (RASREC) Rosetta NMR calcu...

journal_title：Journal of biomolecular NMR

authors： Lange OF

更新日期：2014-07-01 00:00:00

abstract：:Protein-ligand titrations can readily be monitored with a trimethylsilyl (TMS) tag. Owing to the intensity, narrow line shape and unique chemical shift of a TMS group, dissociation constants can be determined from straightforward 1D 1H-NMR spectra not only in the fast but also in the slow exchange limit. The tag is ea...

journal_title：Journal of biomolecular NMR

authors： Becker W,Adams LA,Graham B,Wagner GE,Zangger K,Otting G,Nitsche C

更新日期：2018-04-01 00:00:00

abstract：:The 3D HCCH-TOCSY and HCC(CO)NH-TOCSY experiments provide through bond connectivity and are used for side-chain chemical shift assignment by solution-state NMR. Careful design and implementation of the pulse sequence are key to the successful application of the technique particularly when trying to extract the maximum...

journal_title：Journal of biomolecular NMR

authors： Xia Y,Yuwen T,Rossi P

更新日期：2020-05-01 00:00:00

abstract：:Defining the self-association state of a molecule in solution can be an important step in NMR-based structure determination. This is particularly true of peptides, where there can be a relatively small number of long-range interactions and misinterpretation of an intermolecular NOE as an intramolecular contact can hav...

journal_title：Journal of biomolecular NMR

authors： Yao S,Howlett GJ,Norton RS

更新日期：2000-02-01 00:00:00

abstract：:The P1 adhesin (aka Antigen I/II or PAc) of the cariogenic bacterium Streptococcus mutans is a cell surface-localized protein involved in sucrose-independent adhesion and colonization of the tooth surface. The immunoreactive and adhesive properties of S. mutans suggest an unusual functional quaternary ultrastructure c...

journal_title：Journal of biomolecular NMR

authors： Tang W,Bhatt A,Smith AN,Crowley PJ,Brady LJ,Long JR

更新日期：2016-02-01 00:00:00

abstract：:We present reduced dimensionality (RD) 3D HN(CA)NH for efficient sequential assignment in proteins. The experiment correlates the (15)N and (1)H chemical shift of a residue ('i') with those of its immediate N-terminal (i - 1) and C-terminal (i + 1) neighbors and provides four-dimensional chemical shift correlations ra...

journal_title：Journal of biomolecular NMR

authors： Chandra K,Jaipuria G,Shet D,Atreya HS

更新日期：2012-02-01 00:00:00

abstract：:In this work, we show how the water flip-back approach that is widely employed in solution-state NMR can be adapted to proton-detected MAS solid-state NMR of highly deuterated proteins. The scheme allows to enhance the sensitivity of the experiment by decreasing the recovery time of the proton longitudinal magnetizati...

journal_title：Journal of biomolecular NMR

authors： Chevelkov V,Xiang S,Giller K,Becker S,Lange A,Reif B

更新日期：2015-02-01 00:00:00

abstract：:Recent advances in the field of in-cell NMR spectroscopy have made it possible to study proteins in the context of bacterial or mammalian cell extracts or even entire cells. As most mammalian cells are part of a multi-cellular complex, there is a need to develop novel NMR approaches enabling the study of proteins with...

journal_title：Journal of biomolecular NMR

authors： Damman R,Lucini Paioni A,Xenaki KT,Beltrán Hernández I,van Bergen En Henegouwen PMP,Baldus M

更新日期：2020-09-01 00:00:00

abstract：:TROSY-based triple resonance experiments are essential for protein backbone assignment of large biomolecular systems by solution NMR spectroscopy. In a survey of the current Bruker pulse sequence library for TROSY-based experiments we found that several sequences were plagued by artifacts that affect spectral quality ...

journal_title：Journal of biomolecular NMR

authors： Xia Y,Rossi P,Tonelli M,Huang C,Kalodimos CG,Veglia G

更新日期：2017-09-01 00:00:00

abstract：:We report here the backbone 1HN, 15N, 13C alpha, 13CO, and 1H alpha NMR assignments for the catalytic domain of human fibroblast collagenase (HFC). Three independent assignment pathways (matching 1H, 13C alpha, and 13CO resonances) were used to establish sequential connections. The connections using 13C alpha resonanc...

journal_title：Journal of biomolecular NMR

authors： McCoy MA,Dellwo MJ,Schneider DM,Banks TM,Falvo J,Vavra KJ,Mathiowetz AM,Qoronfleh MW,Ciccarelli R,Cook ER,Pulvino TA,Wahl RC,Wang H

更新日期：1997-01-01 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：:Adiabatic pulses have been widely used for broadband decoupling and spin inversion at high magnetic fields. In this paper we propose adiabatic pulses and supercycles that can be used at high magnetic fields like 800 or 900 MHz to obtain broadband TOCSY sequences with C,C or H,H J-transfer. The new mixing sequences are...

journal_title：Journal of biomolecular NMR

authors： Peti W,Griesinger C,Bermel W

更新日期：2000-11-01 00:00:00

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

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

更新日期：1991-07-01 00:00:00

abstract：:Sample solubility is essential for structural studies of proteins by solution NMR. Attachment of a solubility enhancement tag, such as GB1, MBP and thioredoxin, to a target protein has been used for this purpose. However, signal overlap of the tag with the target protein often made the spectral analysis difficult. Her...

journal_title：Journal of biomolecular NMR

authors： Kobashigawa Y,Kumeta H,Ogura K,Inagaki F

更新日期：2009-03-01 00:00:00

abstract：:The application of metabolic precursors for selective stable isotope labeling of aromatic residues in cell-based protein overexpression has already resulted in numerous NMR probes to study the structural and dynamic characteristics of proteins. With anthranilic acid, we present the structurally simplest precursor for ...

journal_title：Journal of biomolecular NMR

authors： Schörghuber J,Geist L,Bisaccia M,Weber F,Konrat R,Lichtenecker RJ

更新日期：2017-09-01 00:00:00

abstract：:Prerequisite for chemical shift (CS) and CS tensor calculations are highly refined structures defining the molecular surroundings of the nuclei under study. Here, we present geometry optimizations with 13C and 15N CS constraints for large bio-molecules like peptides and proteins. The method discussed here provides bot...

journal_title：Journal of biomolecular NMR

authors： Sternberg U,Witter R

更新日期：2019-12-01 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：: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

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：:Mollib is a software framework for the analysis of molecular structures, properties and data with an emphasis on data collected by NMR. It uses an open source model and a plugin framework to promote community-driven development of new and enhanced features. Mollib includes tools for the automatic retrieval and caching...

journal_title：Journal of biomolecular NMR

authors： Lorieau JL

更新日期：2017-10-01 00:00:00

abstract：:Activated dynamics plays a central role in protein function, where transitions between distinct conformations often underlie the switching between active and inactive states. The characteristic time scales of these transitions typically fall in the microsecond to millisecond range, which is amenable to investigations ...

journal_title：Journal of biomolecular NMR

authors： Weininger U,Blissing AT,Hennig J,Ahlner A,Liu Z,Vogel HJ,Akke M,Lundström P

更新日期：2013-09-01 00:00:00

abstract：:The voltage-dependent anion channel (VDAC) is the most abundant protein of the outer mitochondrial membrane and constitutes the major pathway for the transport of ADP, ATP, and other metabolites. In this multidisciplinary study we combined solid-state NMR, electrophysiology, and molecular dynamics simulations, to stud...

journal_title：Journal of biomolecular NMR

authors： Gattin Z,Schneider R,Laukat Y,Giller K,Maier E,Zweckstetter M,Griesinger C,Benz R,Becker S,Lange A

更新日期：2015-04-01 00:00:00

abstract：:Paramagnetic relaxation enhancement (PRE) measurements constitute a powerful approach for detecting both permanent and transient protein-protein interactions. Typical PRE experiments require an intrinsic or engineered paramagnetic site on one of the two interacting partners; while a second, diamagnetic binding partner...

journal_title：Journal of biomolecular NMR

authors： Olivieri C,Subrahmanian MV,Xia Y,Kim J,Porcelli F,Veglia G

更新日期：2018-03-01 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：:NMR relaxometry plays crucial role in studies of protein dynamics. The measurement of longitudinal and transverse relaxation rates of [Formula: see text]N is the main source of information on backbone motions. However, even the most basic approach exploiting a series of [Formula: see text]N HSQC spectra can require se...

journal_title：Journal of biomolecular NMR

authors： Urbańczyk M,Nowakowski M,Koźmiński W,Kazimierczuk K

更新日期：2017-06-01 00:00:00

abstract：:The use of pulsed field gradients in multiple-pulse NMR experiments has many advantages, including the possibility of obtaining excellent water suppression without the need for selective presaturation. In such gradient experiments the water magnetization is dephased deliberately; exchange between the saturated protons...

journal_title：Journal of biomolecular NMR

authors： Stonehouse J,Clowes RT,Shaw GL,Keeler J,Laue ED

更新日期：1995-04-01 00:00:00

abstract：:Cytochrome c552 from the thermophilic bacterium Hydrogenobacter thermophilus is a typical c-type cytochrome which binds heme covalently via two thioether bonds between the two heme vinyl groups and two cysteine thiol groups in a CXXCH sequence motif. This protein was converted to a b-type cytochrome by substitution of...

journal_title：Journal of biomolecular NMR

authors： Tozawa K,Ferguson SJ,Redfield C,Smith LJ

更新日期：2015-06-01 00:00:00