当前位置： SCI文献检索 > JOURNAL OF BIOMOLECULAR NMR期刊下所有文献 > Sequential correlation of anomeric ribose protons and intervening phosphorus in RNA oligonucleotides by a 1H, 13C, 31P triple resonance experiment: HCP-CCH-TOCSY.

Sequential correlation of anomeric ribose protons and intervening phosphorus in RNA oligonucleotides by a 1H, 13C, 31P triple resonance experiment: HCP-CCH-TOCSY.

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 complete ribose spin system to the intervening phosphorus is obtained by adding a C,C-TOCSY coherence transfer step to the triple resonance HCP experiment. The C,C-TOCSY transfer step, which utilizes the large and relatively uniform 1J(C,C) coupling constant (approximately 40 Hz for ribose carbons), efficiently correlates the phosphorus-coupled carbons observed in the HCP correlation experiment (i.e., C4' and C5' in the 5' direction and C4' and C3' in the 3' direction) to all other carbons in the ribose spin system. Of the additional correlations observed in the HCP-CCH-TOCSY, that to the relatively well-resolved anomeric H1',C1' resonance pairs provides the greatest gain in terms of facilitating assignment. The gain in spectral resolution afforded by chemical shift labeling with the anomeric resonances should provide a more robust pathway for sequential assignment over the intervening phosphorus in larger RNA oligonucleotides. The HCP-CCH-TOCSY experiment is demonstrated on a uniformly 13C, 15N-labeled 19-nucleotide RNA stem-loop, derived from the antisense RNA I molecule found in the ColE1 plasmid replication control system.

journal_name

J Biomol NMR

journal_title

Journal of biomolecular NMR

authors

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

doi

10.1007/BF00227473

subject

Has Abstract

pub_date

1995-01-01 00:00:00

pages

87-92

issue

1

eissn

0925-2738

issn

1573-5001

journal_volume

5

pub_type

杂志文章

相关文献

JOURNAL OF BIOMOLECULAR NMR文献大全
  • Optimized labeling of 13CHD2 methyl isotopomers in perdeuterated proteins: potential advantages for 13C relaxation studies of methyl dynamics of larger proteins.

    abstract：:13CHD2 methyl isotopomers are particularly useful to study methyl dynamics in proteins because, as compared with other methyl isotopomers, the 13C relaxation mechanism for this isotopomer is straightforward. However, in the case of proteins, where (omega tau)2 > 1, the refocused INEPT pulse sequence does not completel...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1023/a:1012482426306

    authors： Ishima R,Louis JM,Torchia DA

    更新日期：2001-10-01 00:00:00

  • Determination of a complete set of coupling constants in 13C-labeled oligonucleotides.

    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

    pub_type： 杂志文章

    doi：10.1007/BF00404274

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

    更新日期：1994-09-01 00:00:00

  • The war of tools: how can NMR spectroscopists detect errors in their structures?

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-008-9228-4

    authors： Saccenti E,Rosato A

    更新日期：2008-04-01 00:00:00

  • Identification of solvent-exposed regions of an FK-506 analog, ascomycin, bound to FKBP using a paramagnetic probe.

    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

    pub_type： 杂志文章

    doi：10.1007/BF02192797

    authors： Petros AM,Neri P,Fesik SW

    更新日期：1992-01-01 00:00:00

  • Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-016-0017-1

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

    更新日期：2016-02-01 00:00:00

  • Automated solvent artifact removal and base plane correction of multidimensional NMR protein spectra by AUREMOL-SSA.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-010-9414-z

    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

  • Quantifying Lipari-Szabo modelfree parameters from 13CO NMR relaxation experiments.

    abstract：:It is proposed to obtain effective Lipari-Szabo order parameters and local correlation times for relaxation vectors of protein (13)CO nuclei by carrying out a (13)CO-R(1) auto relaxation experiment, a transverse (13)CO CSA/13CO-13Calpha CSA/dipolar cross correlation and a transverse (13)CO CSA/(13)CO-(15)N CSA/dipolar...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-006-9047-4

    authors： Wang T,Weaver DS,Cai S,Zuiderweg ER

    更新日期：2006-10-01 00:00:00

  • Direct amide 15N to 13C transfers for solid-state assignment experiments in deuterated proteins.

    abstract：:The assignment of protein backbone and side-chain NMR chemical shifts is the first step towards the characterization of protein structure. The recent introduction of proton detection in combination with fast MAS has opened up novel opportunities for assignment experiments. However, typical 3D sequential-assignment exp...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-018-0207-0

    authors： Lends A,Ravotti F,Zandomeneghi G,Böckmann A,Ernst M,Meier BH

    更新日期：2018-10-01 00:00:00

  • Maximum entropy approach to the determination of solution conformation of flexible polypeptides by global conformational analysis and NMR spectroscopy--application to DNS1-c-[D-A2,bu2,Trp4,Leu5]enkephalin and DNS1-c-[D-A2bu2,Trp4,D-Leu5]enkephalin.

    abstract：:A method is proposed to determine the conformational equilibrium of flexible polypeptides in solution, using the data provided by NMR spectroscopy and theoretical conformational calculations. The algorithm consists of the following three steps: (i) search of the conformational space in order to find conformations with...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1023/a:1008349424452

    authors： Groth M,Malicka J,Czaplewski C,Ołdziej S,Lankiewicz L,Wiczk W,Liwo A

    更新日期：1999-12-01 00:00:00

  • Spin-state selection filters for the measurement of heteronuclear one-bond coupling constants.

    abstract：:Novel alpha/beta-half-filter elements are proposed for the separation of the high-field and low-field component of 1JHC and 1JHN splittings into different subspectra. The alpha/beta-half-filter elements are of the same duration as the S3CT pulse sequence element and, like this, are less sensitive to cross talk between...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1023/a:1008239027287

    authors： Andersson P,Weigelt J,Otting G

    更新日期：1998-10-01 00:00:00

  • 1H-1H correlations across N-H...N hydrogen bonds in nucleic acids.

    abstract：:In 2HJ(NN)-COSY experiments, which correlate protons with donor/acceptor nitrogens across Nd...HNa bonds, the receptor nitrogen needs to be assigned in order to unambiguously identify the hydrogen bond. For many situations this is a non-trivial task which is further complicated by poor dispersion of (Na,Nd) resonances...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1023/a:1013340227140

    authors： Majumdar A,Gosser Y,Patel DJ

    更新日期：2001-12-01 00:00:00

  • Temperature-jump NMR study of protein folding: ribonuclease A at low pH.

    abstract：:The kinetic process of folding of bovine pancreatic ribonuclease A in a 2H2O environment at pH 1.2 was examined by a recently developed temperature-jump NMR method (Akasaka et al., (1990) Rev. Sci. Instrum. 61, 66-68). Upon temperature-jump down from 45 degrees C to 29 degrees C, which was attained within 6 s, the pro...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/BF01874569

    authors： Akasaka K,Naito A,Nakatani H

    更新日期：1991-05-01 00:00:00

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

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-008-9296-5

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

    更新日期：2009-03-01 00:00:00

  • Development and application of aromatic [(13)C, (1)H] SOFAST-HMQC NMR experiment for nucleic acids.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-014-9856-9

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

    更新日期：2014-11-01 00:00:00

  • 13C alpha-NMR assignments of melittin in methanol and chemical shift correlations with secondary structure.

    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

    pub_type： 杂志文章

    doi：10.1007/BF00198369

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

    更新日期：1993-11-01 00:00:00

  • Site-specific labeling of proteins with NMR-active unnatural amino acids.

    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

    pub_type： 杂志文章,评审

    doi：10.1007/s10858-009-9365-4

    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

  • NMR structure determination of proteins supplemented by quantum chemical calculations: detailed structure of the Ca2+ sites in the EGF34 fragment of protein S.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-004-6729-7

    authors： Hsiao YW,Drakenberg T,Ryde U

    更新日期：2005-02-01 00:00:00

  • Comprehensive analysis of NMR data using advanced line shape fitting.

    abstract：:NMR spectroscopy is uniquely suited for atomic resolution studies of biomolecules such as proteins, nucleic acids and metabolites, since detailed information on structure and dynamics are encoded in positions and line shapes of peaks in NMR spectra. Unfortunately, accurate determination of these parameters is often co...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-017-0141-6

    authors： Niklasson M,Otten R,Ahlner A,Andresen C,Schlagnitweit J,Petzold K,Lundström P

    更新日期：2017-10-01 00:00:00

  • In situ NMR measurement of macromolecule-bound metal ion concentrations.

    abstract：:Many nucleic acids and proteins require divalent metal ions such as Mg(2+) and Ca(2+) for folding and function. The lipophilic alignment media frequently used as membrane mimetics also bind these divalent metals. Here we demonstrate the use of (31)P NMR spectrum of a metal ion chelator (deoxycytidine diphosphate) to m...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-016-0031-3

    authors： Kozlyuk N,Sengupta S,Lupták A,Martin RW

    更新日期：2016-04-01 00:00:00

  • Isotope labeling of mammalian GPCRs in HEK293 cells and characterization of the C-terminus of bovine rhodopsin by high resolution liquid NMR spectroscopy.

    abstract：:High amino acid coverage labeling of the mammalian G protein coupled receptors (GPCR) rhodopsin was established with 15N and 15N/13C isotopes. Rhodopsin was expressed at preparative scale in HEK293S cells and studied in full-length by NMR spectroscopy in detergent micelle solution. This resulted in the assignment and ...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-007-9205-3

    authors： Werner K,Richter C,Klein-Seetharaman J,Schwalbe H

    更新日期：2008-01-01 00:00:00

  • A single-quantum methyl 13C-relaxation dispersion experiment with improved sensitivity.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-007-9149-7

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

    更新日期：2007-05-01 00:00:00

  • A chemical approach for site-specific identification of NMR signals from protein side-chain NH₃⁺ groups forming intermolecular ion pairs in protein-nucleic acid complexes.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-015-9909-8

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

    更新日期：2015-05-01 00:00:00

  • 1H NMR studies of deuterated ribonuclease HI selectively labeled with protonated amino acids.

    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

    pub_type： 杂志文章

    doi：10.1007/BF01875525

    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

  • Insight into human insulin aggregation revisited using NMR derived translational diffusion parameters.

    abstract：:The NMR derived translational diffusion coefficients were performed on unlabeled and uniformly labeled 13C,15N human insulin in water, both in neat, with zinc ions only, and in pharmaceutical formulation, containing only m-cresol as phenolic ligand, glycerol and zinc ions. The results show the dominant role of the pH ...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-018-0197-y

    authors： Sitkowski J,Bocian W,Bednarek E,Urbańczyk M,Koźmiński W,Borowicz P,Płucienniczak G,Łukasiewicz N,Sokołowska I,Kozerski L

    更新日期：2018-06-01 00:00:00

  • Rapid measurement of long-range distances in proteins by multidimensional 13C-19F REDOR NMR under fast magic-angle spinning.

    abstract：:The ability to simultaneously measure many long-range distances is critical to efficient and accurate determination of protein structures by solid-state NMR (SSNMR). So far, the most common distance constraints for proteins are 13C-15N distances, which are usually measured using the rotational-echo double-resonance (R...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-018-0187-0

    authors： Shcherbakov AA,Hong M

    更新日期：2018-05-01 00:00:00

  • Solution structure of the soluble domain of the NfeD protein YuaF from Bacillus subtilis.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-008-9261-3

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

    更新日期：2008-09-01 00:00:00

  • Theoretical framework for NMR residual dipolar couplings in unfolded proteins.

    abstract：:A theoretical framework for the prediction of nuclear magnetic resonance (NMR) residual dipolar couplings (RDCs) in unfolded proteins under weakly aligning conditions is presented. The unfolded polypeptide chain is modeled as a random flight chain while the alignment medium is represented by a set of regularly arrange...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-007-9169-3

    authors： Obolensky OI,Schlepckow K,Schwalbe H,Solov'yov AV

    更新日期：2007-09-01 00:00:00

  • Stable isotope labeling approaches for NMR characterization of glycoproteins using eukaryotic expression systems.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-018-0169-2

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

    更新日期：2018-07-01 00:00:00

  • Combined use of 13C chemical shift and 1H alpha-13C alpha heteronuclear NOE data in monitoring a protein NMR structure refinement.

    abstract：:A large portion of the 13C resonance assignments for murine epidermal growth factor (mEGF) at pH 3.1 and 28 degrees C has been determined at natural isotope abundance. Sequence-specific 13C assignments are reported for 100% of the assignable C alpha, 96% of the C beta, 86% of the aromatic and 70% of the remaining peri...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/BF00208807

    authors： Celda B,Biamonti C,Arnau MJ,Tejero R,Montelione GT

    更新日期：1995-02-01 00:00:00

  • Off-resonance effects in 15N T2 CPMG measurements.

    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

    pub_type： 杂志文章

    doi：10.1023/a:1008348827208

    authors： Korzhnev DM,Tischenko EV,Arseniev AS

    更新日期：2000-07-01 00:00:00