当前位置： SCI文献检索 > JOURNAL OF BIOMOLECULAR NMR期刊下所有文献 > Triple resonance ¹⁵Ν NMR relaxation experiments for studies of intrinsically disordered proteins.

Triple resonance ¹⁵Ν NMR relaxation experiments for studies of intrinsically disordered proteins.

Abstract：

:Description of protein dynamics is known to be essential in understanding their function. Studies based on a well established [Formula: see text] NMR relaxation methodology have been applied to a large number of systems. However, the low dispersion of [Formula: see text] chemical shifts very often observed within intrinsically disordered proteins complicates utilization of standard 2D HN correlated spectra because a limited number of amino acids can be characterized. Here we present a suite of triple resonance HNCO-type NMR experiments for measurements of five [Formula: see text] relaxation parameters ([Formula: see text], [Formula: see text], NOE, cross-correlated relaxation rates [Formula: see text] and [Formula: see text]) in doubly [Formula: see text],[Formula: see text]-labeled proteins. We show that the third spectral dimension combined with non-uniform sampling provides relaxation rates for almost all residues of a protein with extremely poor chemical shift dispersion, the C terminal domain of [Formula: see text]-subunit of RNA polymerase from Bacillus subtilis. Comparison with data obtained using a sample labeled by [Formula: see text] only showed that the presence of [Formula: see text] has a negligible effect on [Formula: see text], [Formula: see text], and on the cross-relaxation rate (calculated from NOE and [Formula: see text]), and that these relaxation rates can be used to calculate accurate spectral density values. Partially [Formula: see text]-labeled sample was used to test if the observed increase of [Formula: see text] [Formula: see text] in the presence of [Formula: see text] corresponds to the [Formula: see text] dipole-dipole interactions in the [Formula: see text],[Formula: see text]-labeled sample.

journal_name

J Biomol NMR

journal_title

Journal of biomolecular NMR

authors

Srb P,Nováček J,Kadeřávek P,Rabatinová A,Krásný L,Žídková J,Bobálová J,Sklenář V,Žídek L

doi

10.1007/s10858-017-0138-1

subject

Has Abstract

pub_date

2017-11-01 00:00:00

pages

133-146

issue

3

eissn

0925-2738

issn

1573-5001

pii

10.1007/s10858-017-0138-1

journal_volume

69

pub_type

杂志文章

相关文献

JOURNAL OF BIOMOLECULAR NMR文献大全
  • Resolution-enhanced base-type-edited HCN experiment for RNA.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-005-8872-1

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

    更新日期：2005-08-01 00:00:00

  • Cross-correlation suppressed T1 and NOE experiments for protein side-chain 13CH2 groups.

    abstract：:Relaxation measurements of side-chain 13CH2-groups of uniformly 13C labeled human ubiquitin were performed at 600 MHz and 800 MHz magnetic field strength at 30 degrees C. Dipole-dipole cross-correlated relaxation effects in T1 experiments were suppressed by the combination of radio-frequency pulses and pulsed field gr...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1023/a:1023833407515

    authors： Jin C,Prompers JJ,Brüschweiler R

    更新日期：2003-07-01 00:00:00

  • NMR of bicelles: orientation and mosaic spread of the liquid-crystal director under sample rotation.

    abstract：:Model-membrane systems composed of liquid-crystalline bicellar phases can be uniaxially oriented with respect to a magnetic field, thereby facilitating structural and dynamics studies of membrane-associated proteins. Here we quantitatively characterize a method that allows the manipulation of the direction of this uni...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1023/a:1022236217018

    authors： Zandomeneghi G,Tomaselli M,Williamson PT,Meier BH

    更新日期：2003-02-01 00:00:00

  • Solid state NMR sequential resonance assignments and conformational analysis of the 2x10.4 kDa dimeric form of the Bacillus subtilis protein Crh.

    abstract：:Solid state NMR sample preparation and resonance assignments of the U-[13C,15N] 2x10.4 kDa dimeric form of the regulatory protein Crh in microcrystalline, PEG precipitated form are presented. Intra- and interresidue correlations using dipolar polarization transfer methods led to nearly complete sequential assignments ...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1023/a:1025820611009

    authors： Böckmann A,Lange A,Galinier A,Luca S,Giraud N,Juy M,Heise H,Montserret R,Penin F,Baldus M

    更新日期：2003-12-01 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

  • [13C]-constant-time [15N,1H]-TROSY-HNCA for sequential assignments of large proteins.

    abstract：:The greatly improved sensitivity resulting from the use of TROSY during 15N evolution and amide proton acquisition enables the recording of HNCA spectra of large proteins with constant-time 13C alpha evolution. In [13C]-ct-[15N,1H]-TROSY-HNCA experiments with a 2H/13C/15N-labeled 110 kDa protein, 7,8-dihydroneopterin ...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1023/a:1008346931993

    authors： Salzmann M,Pervushin K,Wider G,Senn H,Wüthrich K

    更新日期：1999-05-01 00:00:00

  • (31)P NMR correlation maps of (18)O/ (16)O chemical shift isotopic effects for phosphometabolite labeling studies.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-011-9515-3

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

    更新日期：2011-07-01 00:00:00

  • GFT projection NMR based resonance assignment of membrane proteins: application to subunit C of E. coli F(1)F (0) ATP synthase in LPPG micelles.

    abstract：:G-matrix FT projection NMR spectroscopy was employed for resonance assignment of the 79-residue subunit c of the Escherichia coli F(1)F(0) ATP synthase embedded in micelles formed by lyso palmitoyl phosphatidyl glycerol (LPPG). Five GFT NMR experiments, that is, (3,2)D HNNCO, L-(4,3)D HNNC (alphabeta) C (alpha), L-(4,...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-008-9224-8

    authors： Zhang Q,Atreya HS,Kamen DE,Girvin ME,Szyperski T

    更新日期：2008-03-01 00:00:00

  • Importance of time-ordered non-uniform sampling of multi-dimensional NMR spectra of Aβ1-42 peptide under aggregating conditions.

    abstract：:Although the order of the time steps in which the non-uniform sampling (NUS) schedule is implemented when acquiring multi-dimensional NMR spectra is of limited importance when sample conditions remain unchanged over the course of the experiment, it is shown to have major impact when samples are unstable. In the latter...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-019-00235-7

    authors： Ying J,Barnes CA,Louis JM,Bax A

    更新日期：2019-09-01 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

  • Proton, carbon, and nitrogen chemical shifts accurately delineate differences and similarities in secondary structure between the homologous proteins IRAP and IL-1 beta.

    abstract：:1H alpha, 13C alpha, and 15N alpha secondary shifts, defined as the difference between the observed value and the random coil value, have been calculated for interleukin-1 receptor antagonist protein and interleukin-1 beta. Averaging of the secondary chemical shifts with those of adjacent residues was used to smooth o...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/BF02192848

    authors： Stockman BJ,Scahill TA,Strakalaitis NA,Brunner DP,Yem AW,Deibel MR Jr

    更新日期：1992-11-01 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

  • The use of chemical shift temperature gradients to establish the paramagnetic susceptibility tensor orientation: implication for structure determination/refinement in paramagnetic metalloproteins.

    abstract：:The use of dipolar shifts as important constraints in refining molecular structure of paramagnetic metalloproteins by solution NMR is now well established. A crucial initial step in this procedure is the determination of the orientation. of the anisotropic paramagnetic susceptibility tensor in the molecular frame whic...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1023/a:1008309121949

    authors： Xia Z,Nguyen BD,La Mar GN

    更新日期：2000-06-01 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

  • Investigation of backbone dynamics and local geometry of bio-molecules using calculated NMR chemical shifts and anisotropies.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-019-00284-y

    authors： Sternberg U,Witter R

    更新日期：2019-12-01 00:00:00

  • Estimates of methyl 13C and 1H CSA values (Deltasigma) in proteins from cross-correlated spin relaxation.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-004-4349-x

    authors： Tugarinov V,Scheurer C,Brüschweiler R,Kay LE

    更新日期：2004-12-01 00:00:00

  • Segmental isotopic labeling by asparaginyl endopeptidase-mediated protein ligation.

    abstract：:Segmental isotopic labeling can facilitate NMR studies of large proteins, multi-domain proteins, and proteins with repetitive sequences by alleviating NMR signal overlaps. Segmental isotopic labeling also allows us to investigate an individual domain in the context of a full-length protein by NMR. Several established ...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-018-0175-4

    authors： Mikula KM,Krumwiede L,Plückthun A,Iwaï H

    更新日期：2018-08-01 00:00:00

  • Automatic NOESY assignment in CS-RASREC-Rosetta.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-014-9833-3

    authors： Lange OF

    更新日期：2014-07-01 00:00:00

  • Definition of a new information-based per-residue quality parameter.

    abstract：:For biomolecular NMR structures typically only a poor correspondence is observed between statistics derived from the experimental input data and structural quality indicators obtained from the structure ensembles. Here, we investigate the relationship between the amount of available NMR data and structure quality. By ...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-005-2826-5

    authors： Nabuurs SB,Krieger E,Spronk CA,Nederveen AJ,Vriend G,Vuister GW

    更新日期：2005-10-01 00:00:00

  • Simultaneous detection of intra- and inter-molecular paramagnetic relaxation enhancements in protein complexes.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-018-0165-6

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

    更新日期：2018-03-01 00:00:00

  • Adiabatic heteronuclear decoupling in rotating solids.

    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

    pub_type： 杂志文章

    doi：10.1023/B:JNMR.0000032614.79833.3d

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

    更新日期：2004-07-01 00:00:00

  • Optimization of amino acid type-specific 13C and 15N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm.

    abstract：:We present a computational method for finding optimal labeling patterns for the backbone assignment of membrane proteins and other large proteins that cannot be assigned by conventional strategies. Following the approach of Kainosho and Tsuji (Biochemistry 21:6273-6279 (1982)), types of amino acids are labeled with (1...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-010-9462-4

    authors： Hefke F,Bagaria A,Reckel S,Ullrich SJ,Dötsch V,Glaubitz C,Güntert P

    更新日期：2011-02-01 00:00:00

  • Automated evaluation of chemical shift perturbation spectra: New approaches to quantitative analysis of receptor-ligand interaction NMR spectra.

    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

    pub_type： 杂志文章

    doi：10.1023/B:JNMR.0000034351.37982.9e

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

    更新日期：2004-08-01 00:00:00

  • Trans-hydrogen bond deuterium isotope effects of A:T base pairs in DNA.

    abstract：:The chemical shifts of (13)C2 of adenosine residues of DNA were observed to experience a through-space or trans-hydrogen bond isotope effect as a result of deuterium substitution at the imino hydrogen site of base-paired thymidine residues. NMR measurements of several self-complementary DNA duplexes at natural abundan...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1023/B:JNMR.0000019507.95667.3e

    authors： Vakonakis I,LiWang AC

    更新日期：2004-05-01 00:00:00

  • Interaction of the tail with the catalytic region of a class II E2 conjugating enzyme.

    abstract：:Ubiquitination plays an important role in many biological processes, including DNA repair, cell cycle regulation, and protein degradation. In the latter pathway the ubiquitin-conjugating enzymes or E2 enzymes are important proteins forming a key E2-ubiquitin thiolester prior to substrate labelling. While the structure...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1023/a:1023571703783

    authors： Merkley N,Shaw GS

    更新日期：2003-06-01 00:00:00

  • Al NMR: a novel NMR data processing program optimized for sparse sampling.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-011-9584-3

    authors： Gledhill JM Jr,Wand AJ

    更新日期：2012-01-01 00:00:00

  • Amide temperature coefficients in the protein G B1 domain.

    abstract：:Temperature coefficients have been measured for backbone amide (1)H and (15)N nuclei in the B1 domain of protein G (GB1), using temperatures in the range 283-313 K, and pH values from 2.0 to 9.0. Many nuclei display pH-dependent coefficients, which were fitted to one or two pK(a) values. (1)H coefficients showed the e...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-011-9583-4

    authors： Tomlinson JH,Williamson MP

    更新日期：2012-01-01 00:00:00

  • Cross-correlated spin relaxation effects in methyl 1H CPMG-based relaxation dispersion experiments: complications and a simple solution.

    abstract：:Artifacts associated with the measurement of methyl (1)H single quantum CPMG-based relaxation dispersion profiles are described. These artifacts arise due to the combination of cross-correlated spin relaxation effects involving intra-methyl (1)H-(1)H dipolar interactions and imperfections in (1)H refocusing pulses tha...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-005-2468-7

    authors： Korzhnev DM,Mittermaier AK,Kay LE

    更新日期：2005-04-01 00:00:00

  • Complete assignment of 1H, 13C and 15N chemical shifts for bovine beta-lactoglobulin: secondary structure and topology of the native state is retained in a partially unfolded form.

    abstract：:Although beta-lactoglobulin (beta-LG) has been studied extensively for more than 50 years, its physical properties in solution are not yet understood fully in terms of its three-dimensional (3D) structure. For example, despite a recent high-resolution crystal structure, it is still not clear why the two common variant...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1023/a:1008268528695

    authors： Uhrínová S,Uhrín D,Denton H,Smith M,Sawyer L,Barlow PN

    更新日期：1998-07-01 00:00:00

  • NMR-based metabolomics of mammalian cell and tissue cultures.

    abstract：:NMR spectroscopy was used to evaluate growth media and the cellular metabolome in two systems of interest to biomedical research. The first of these was a Chinese hamster ovary cell line engineered to express a recombinant protein. Here, NMR spectroscopy and a quantum mechanical total line shape analysis were utilized...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-011-9490-8

    authors： Aranibar N,Borys M,Mackin NA,Ly V,Abu-Absi N,Abu-Absi S,Niemitz M,Schilling B,Li ZJ,Brock B,Russell RJ 2nd,Tymiak A,Reily MD

    更新日期：2011-04-01 00:00:00