当前位置： SCI文献检索 > JOURNAL OF BIOMOLECULAR NMR期刊下所有文献 > Determination of the relative NH proton lifetimes of the peptide analogue viomycin in aqueous solution by NMR-based diffusion measurement.

Determination of the relative NH proton lifetimes of the peptide analogue viomycin in aqueous solution by NMR-based diffusion measurement.

Abstract：

:In aqueous solution, exchanging peptide NH protons experience two environments, that of the peptide itself with a relatively slow diffusion coefficient and that of the water solvent with a faster diffusion coefficient. Although in slow exchange on the NMR chemical shift timescale, the magnetic field gradient dependence of the NH peak intensities in an experiment used to measure diffusion coefficients reflects the relative time periods spent in the two environments and this allows the determination of the relative solvent accessibility of exchangeable protons in peptides or proteins. To test this approach, the magnetic field gradient dependent intensities of the chemically shifted amide and amine NH protons of the peptide antibiotic viomycin have been measured using the high resolution longitudinal-eddy-current-delay (LED) NMR method incorporating solvent water peak elimination by non-excitation. The NH resonances of viomycin have been assigned previously and their relative exchange rates determined. Here, the gradient dependence of each NH proton intensity is reported, and these, after a bi- exponential least squares fitting, yield the fractional lifetimes of the protons spent in the peptide and water environments during the diffusion period of the experiment.

journal_name

J Biomol NMR

journal_title

Journal of biomolecular NMR

authors

Liu M,Toms HC,Hawkes GE,Nicholson JK,Lindon JC

doi

10.1023/A:1008393202076

subject

Has Abstract

pub_date

1999-01-01 00:00:00

pages

25-30

issue

1

eissn

0925-2738

issn

1573-5001

journal_volume

13

pub_type

杂志文章

相关文献

JOURNAL OF BIOMOLECULAR NMR文献大全
  • 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

  • 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

  • Improved NMR spectra of a protein-DNA complex through rational mutagenesis and the application of a sensitivity optimized isotope-filtered NOESY experiment.

    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

    pub_type： 杂志文章

    doi：10.1023/a:1011296112710

    authors： Iwahara J,Wojciak JM,Clubb RT

    更新日期：2001-03-01 00:00:00

  • 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 intr...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-017-0138-1

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

    更新日期：2017-11-01 00:00:00

  • Efficient analysis of protein 2D NMR spectra using the software package EASY.

    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

    pub_type： 杂志文章

    doi：10.1007/BF01877224

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

    更新日期：1991-07-01 00:00:00

  • Ensembles of a small number of conformations with relative populations.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-015-9993-9

    authors： Vammi V,Song G

    更新日期：2015-12-01 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

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

    abstract：:S3EPY is a Python extension to the program Sparky written to facilitate the assessment of coupling constants from in-phase/antiphase and spin-state-selective excitation (S(3)E) experiments. It enables the routine use of small scalar couplings by automating the coupling evaluation procedure. S3EPY provides an integrate...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-009-9392-1

    authors： Novák P,Zídek L,Motácková V,Padrta P,Svenková A,Nuzillard JM,Krásný L,Sklenár V

    更新日期：2010-02-01 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

  • 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

  • Characterizing the magnetic susceptibility tensor of lanthanide-containing polymethylated-DOTA complexes.

    abstract：:Lanthanide complexes based on the DOTA (1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid) cage are commonly used as phase contrast agents in magnetic resonance imaging, but can also be utilized in structural NMR applications due to their ability to induce either paramagnetic relaxation enhancement or a pseudoc...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-016-0061-x

    authors： Strickland M,Schwieters CD,Göbl C,Opina AC,Strub MP,Swenson RE,Vasalatiy O,Tjandra N

    更新日期：2016-10-01 00:00:00

  • Improved segmental isotope labeling of proteins and application to a larger protein.

    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

    pub_type： 杂志文章

    doi：10.1023/a:1008308128050

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

    更新日期：1999-06-01 00:00:00

  • 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

  • Structural features of the metal binding site and dynamics of gallium putidaredoxin, a diamagnetic derivative of a Cys4Fe2S2 ferredoxin.

    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

    pub_type： 杂志文章

    doi：10.1023/a:1018369721091

    authors： Kazanis S,Pochapsky TC

    更新日期：1997-06-01 00:00:00

  • Parametrisation of time-averaged distance restraints in MD simulations.

    abstract：:Time-averaged restraints in molecular dynamics simulations offer a means to account for the averaging that is implicit in NMR spectroscopic data. We present a systematic investigation of the parameters which characterise time-averaged distance restraints. Using previously published data for a small protein, chymotryps...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/BF00197812

    authors： Nanzer AP,van Gunsteren WF,Torda AE

    更新日期：1995-11-01 00:00:00

  • Resolution-optimized NMR measurement of (1)D(CH), (1)D(CC) and (2)D(CH) residual dipolar couplings in nucleic acid bases.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-005-1846-5

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

    更新日期：2004-11-01 00:00:00

  • Assignments and structure determination of the catalytic domain of human fibroblast collagenase using 3D double and triple resonance NMR spectroscopy.

    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

    pub_type： 杂志文章

    doi：10.1023/a:1018615400129

    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

  • An improved double-tuned and isotope-filtered pulse scheme based on a pulsed field gradient and a wide-band inversion shaped pulse.

    abstract：:We have developed an improved isotope-filtered pulse scheme in combination with a double-tuned filter, a hyperbolic secant inversion pulse, and a z-filter with a pulsed field gradient. These filtering pulse schemes have been incorporated into several one-, two-, and three-dimensional experiments, which were applied to...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/BF00228150

    authors： Ogura K,Terasawa H,Inagaki F

    更新日期：1996-12-01 00:00:00

  • IBIS--a tool for automated sequential assignment of protein spectra from triple resonance experiments.

    abstract：:We have developed a tool for computer-assisted assignments of protein NMR spectra from triple resonance data. The program is designed to resemble established manual assignment procedures as closely as possible. IBIS exports its results in XEASY format. Thus, using IBIS the operator has continuous visual and accounting...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1023/a:1024078926886

    authors： Hyberts SG,Wagner G

    更新日期：2003-08-01 00:00:00

  • Measuring hydrogen exchange in proteins by selective water saturation in (1)H- (15)N SOFAST/BEST-type experiments: advantages and limitations.

    abstract：:HET(ex)-SOFAST NMR (Schanda et al. in J Biomol NMR 33:199-211, 2006) has been proposed some years ago as a fast and sensitive method for semi-quantitative measurement of site-specific amide-water hydrogen exchange effects along the backbone of proteins. Here we extend this concept to BEST readout sequences that provid...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-014-9857-8

    authors： Rennella E,Solyom Z,Brutscher B

    更新日期：2014-11-01 00:00:00

  • Amino acid type-selective backbone 1H-15N-correlations for Arg and Lys.

    abstract：:Four novel amino acid type-selective triple resonance experiments to identify the backbone amino proton and nitrogen resonances of Arg and Lys and of their sequential neighbors in (13C,15N)-labeled proteins are presented: the R(i+1)-HSQC and R(i,i+1)-HSQC select signals originating from Arg side chains, the K(i+1)-HSQ...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1023/a:1011206131623

    authors： Schubert M,Oschkinat H,Schmieder P

    更新日期：2001-08-01 00:00:00

  • Pulse EPR-enabled interpretation of scarce pseudocontact shifts induced by lanthanide binding tags.

    abstract：:Pseudocontact shifts (PCS) induced by tags loaded with paramagnetic lanthanide ions provide powerful long-range structure information, provided the location of the metal ion relative to the target protein is known. Usually, the metal position is determined by fitting the magnetic susceptibility anisotropy (Δχ) tensor ...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-015-0003-z

    authors： Abdelkader EH,Yao X,Feintuch A,Adams LA,Aurelio L,Graham B,Goldfarb D,Otting G

    更新日期：2016-01-01 00:00:00

  • NMR resonance assignments for sparsely 15N labeled proteins.

    abstract：:For larger proteins, and proteins not amenable to expression in bacterial hosts, it is difficult to deduce structures using NMR methods based on uniform (13)C, (15)N isotopic labeling and observation of just nuclear Overhauser effects (NOEs). In these cases, sparse labeling with selected (15)N enriched amino acids and...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-007-9159-5

    authors： Feng L,Lee HS,Prestegard JH

    更新日期：2007-07-01 00:00:00

  • Stable isotope labeling of glycoprotein expressed in silkworms using immunoglobulin G as a test molecule.

    abstract：:Silkworms serve as promising bioreactors for the production of recombinant proteins, including glycoproteins and membrane proteins, for structural and functional protein analyses. However, lack of methodology for stable isotope labeling has been a major deterrent to using this expression system for nuclear magnetic re...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-015-9930-y

    authors： Yagi H,Nakamura M,Yokoyama J,Zhang Y,Yamaguchi T,Kondo S,Kobayashi J,Kato T,Park EY,Nakazawa S,Hashii N,Kawasaki N,Kato K

    更新日期：2015-06-01 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

  • 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

  • Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R(1ρ): an application to αB-crystallin.

    abstract：:Carr-Purcell-Meiboom-Gill relaxation dispersion (CPMG RD) NMR spectroscopy has emerged as a powerful tool for quantifying the kinetics and thermodynamics of millisecond time-scale exchange processes involving the interconversion between a visible ground state and one or more minor, sparsely populated invisible 'excite...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-012-9617-6

    authors： Baldwin AJ,Kay LE

    更新日期：2012-05-01 00:00:00

  • Understanding and solving abnormal peak splitting in 3D HCCH-TOCSY and HCC(CO)NH-TOCSY.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-020-00310-4

    authors： Xia Y,Yuwen T,Rossi P

    更新日期：2020-05-01 00:00:00

  • SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds.

    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

    pub_type： 杂志文章

    doi：10.1007/s10858-005-4425-x

    authors： Schanda P,Kupce E,Brutscher B

    更新日期：2005-12-01 00:00:00

  • Complexity of aromatic ring-flip motions in proteins: Y97 ring dynamics in cytochrome c observed by cross-relaxation suppressed exchange NMR spectroscopy.

    abstract：:Dynamics of large-amplitude conformational motions in proteins are complex and less understood, although these processes are intimately associated with structure, folding, stability, and function of proteins. Here, we use a large set of spectra obtained by cross-relaxation suppressed exchange NMR spectroscopy (EXSY) t...

    journal_title：Journal of biomolecular NMR

    pub_type： 杂志文章

    doi：10.1007/s10858-007-9186-2

    authors： Rao DK,Bhuyan AK

    更新日期：2007-11-01 00:00:00