Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method.

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：: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：:Intramolecular correlations among the (18)O-labels of metabolic oligophosphates, mapped by J-decoupled (31)P NMR 2D chemical shift correlation spectroscopy, impart stringent constraints to the (18)O-isotope distributions over the whole oligophosphate moiety. The multiple deduced correlations of isotopic labels enable ...

journal_title：Journal of biomolecular NMR

authors： Juranić N,Nemutlu E,Zhang S,Dzeja P,Terzic A,Macura S

更新日期：2011-07-01 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：:New base-type-edited transverse-relaxation optimized CT-HCN(C) experiments are presented that yield intra-base and sugar-to-base correlations for 13C-15N labeled RNA. High spectral resolution in the 13C and 15N dimensions is achieved by constant time (CT) frequency editing. A spectral editing filter applied during the...

journal_title：Journal of biomolecular NMR

authors： Van Melckebeke H,Pardi A,Boisbouvier J,Simorre JP,Brutscher B

更新日期：2005-08-01 00:00:00

abstract：:The first reconstitution of an Fe2S2 ferredoxin with a diamagnetic prosthetic group was recently described [Kazanis et al. (1995) J. Am. Chem. Soc., 117, 6625-6626]. The replacement of the iron-sulfur cluster of the bacterial ferredoxin putidaredoxin (Pdx) by gallium (Ga3+) renders the protein diamagnetic and permits ...

journal_title：Journal of biomolecular NMR

authors： Kazanis S,Pochapsky TC

更新日期：1997-06-01 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：:2D 15N-1H correlation spectra are ideal for measuring backbone amide populations to determine amide exchange protection factors in studies of protein folding or other structural features. Most protein NMR spectroscopists use HSQC, which has been shown to be generally superior to HMQC in both resolution and sensitivity...

journal_title：Journal of biomolecular NMR

authors： Davis JH

更新日期：1995-06-01 00:00:00

abstract：:We demonstrate a novel methodology to disrupt the symmetry in the NMR spectra of homodimers. A paramagnetic probe is introduced sub-stoichiometrically to create an asymmetric system with the paramagnetic probe residing on only one monomer within the dimer. This creates sufficient magnetic anisotropy for resolution of ...

journal_title：Journal of biomolecular NMR

authors： Gaponenko V,Altieri AS,Li J,Byrd RA

更新日期：2002-10-01 00:00:00

abstract：:An approach for the efficient implementation of RN(n)(nu) symmetry-based pulse schemes that are often employed for recoupling and decoupling of nuclear spin interactions in biological solid state NMR investigations is demonstrated at high magic-angle spinning frequencies. RF pulse sequences belonging to the RN(n)(nu) ...

journal_title：Journal of biomolecular NMR

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

更新日期：2009-08-01 00:00:00

abstract：:A pulse sequence is described for recording single-quantum (13)C-methyl relaxation dispersion profiles of (13)C-selectively labeled methyl groups in proteins that offers significant improvements in sensitivity relative to existing approaches where initial magnetization derives from (13)C polarization. Sensitivity gain...

journal_title：Journal of biomolecular NMR

authors： Lundström P,Vallurupalli P,Religa TL,Dahlquist FW,Kay LE

更新日期：2007-05-01 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：: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：:We describe a new labeling method that allows for full protonation at the backbone Hα position, maintaining protein side chains with a high level of deuteration. We refer to the method as alpha proton exchange by transamination (α-PET) since it relies on transaminase activity demonstrated here using Escherichia coli e...

journal_title：Journal of biomolecular NMR

authors： Movellan KT,Najbauer EE,Pratihar S,Salvi M,Giller K,Becker S,Andreas LB

更新日期：2019-02-01 00:00:00

abstract：:Extensive spectral overlap presents a major problem for the NMR study of large RNAs. Here we present NMR techniques for resolution enhancement and spectral simplification of fully 13C labelled RNA. High-resolution 1H-13C correlation spectra are obtained by combining TROSY-type experiments with multiple-band-selective ...

journal_title：Journal of biomolecular NMR

authors： Brutscher B,Boisbouvier J,Kupce E,Tisné C,Dardel F,Marion D,Simorre JP

更新日期：2001-02-01 00:00:00

abstract：:Great theoretical and methodological advances are pushing the limits of resolution and sensitivity in solid state NMR (SSNMR). However, sample preparation remains a critical issue for the success of an experiment. The factors affecting spectral quality in SSNMR samples are discussed, examining cases encountered in the...

journal_title：Journal of biomolecular NMR

authors： Fragai M,Luchinat C,Parigi G,Ravera E

更新日期：2013-10-01 00:00:00

abstract：:Coherences were observed between 15N3 of cytosine and its trans amino proton (H42) using a modified gradient-based heteronuclear single quantum coherence (HSQC) pulse sequence optimized for three-bond proton-nitrogen couplings. The method is demonstrated with a 22-nucleotide RNA fragment of the P5abc region of a group...

journal_title：Journal of biomolecular NMR

authors： Rüdisser S,Pelton JG,Tinoco I Jr

更新日期：1999-10-01 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 describe a novel method for the robust, rapid, and reliable determination of J couplings in multi-dimensional NMR coupling data, including small couplings from larger proteins. The method, "High-resolution Iterative Frequency Identification of Couplings" (HIFI-C) is an extension of the adaptive and intelligent data...

journal_title：Journal of biomolecular NMR

authors： Cornilescu G,Bahrami A,Tonelli M,Markley JL,Eghbalnia HR

更新日期：2007-08-01 00:00:00

abstract：:A new pulse sequence is presented for the measurement of relaxation dispersion profiles quantifying millisecond time-scale exchange dynamics of side-chain carbonyl groups in uniformly (13)C labeled proteins. The methodology has been tested using the 87-residue colicin E7 immunity protein, Im7, which is known to fold v...

journal_title：Journal of biomolecular NMR

authors： Hansen AL,Kay LE

更新日期：2011-08-01 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：:The cryogenic temperatures at which dynamic nuclear polarization (DNP) solid-state NMR experiments need to be carried out cause line-broadening, an effect that is especially detrimental for crowded protein spectra. By increasing the magnetic field strength from 600 to 800 MHz, the resolution of DNP spectra of type III...

journal_title：Journal of biomolecular NMR

authors： Fricke P,Mance D,Chevelkov V,Giller K,Becker S,Baldus M,Lange A

更新日期：2016-08-01 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：: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：:A new isotope labeling technique for peptide segments in a protein sample was recently established using the protein splicing element intein [Yamazaki et al. (1998) J. Am. Chem. Soc., 120, 5591-5592]. This method makes it possible to observe signals of a selected amino (N-) or carboxyl (C-) terminal region along a pep...

journal_title：Journal of biomolecular NMR

authors： Otomo T,Teruya K,Uegaki K,Yamazaki T,Kyogoku Y

更新日期：1999-06-01 00:00:00

abstract：:Protein molecules sample different conformations in solution and characterizing these conformations is crucial to understanding protein function. 15N CEST experiments are now routinely used to study slow conformational exchange of protein molecules between a 'visible' major state and 'invisible' minor states. These ex...

journal_title：Journal of biomolecular NMR

authors： Tiwari VP,Pandit S,Vallurupalli P

更新日期：2019-02-01 00:00:00

abstract：:Higher sensitivity of NMR spectrometers and novel isotopic labeling schemes have ushered the development of rapid data acquisition methodologies, improving the time resolution with which NMR data can be acquired. For nucleic acids, longitudinal relaxation optimization in conjunction with Ernst angle excitation (SOFAST...

journal_title：Journal of biomolecular NMR

authors： Sathyamoorthy B,Lee J,Kimsey I,Ganser LR,Al-Hashimi H

更新日期：2014-11-01 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 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

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

更新日期：1992-03-01 00:00:00