A general Monte Carlo/simulated annealing algorithm for resonance assignment in NMR of uniformly labeled biopolymers.

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：: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

authors： Majumdar A,Gosser Y,Patel DJ

更新日期：2001-12-01 00:00:00

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

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

更新日期：2003-02-01 00:00:00

abstract：:One of the major bottlenecks in the determination of proteinstructures by NMR is in the evaluation of the data produced by theexperiments. An important step in this process is assignment, where thepeaks in the spectra are assigned to specific spins within specificresidues. In this paper, we discuss a spin system assig...

journal_title：Journal of biomolecular NMR

authors： Croft D,Kemmink J,Neidig KP,Oschkinat H

更新日期：1997-10-01 00:00:00

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

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

更新日期：2004-08-01 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：:Residual dipolar couplings (RDC) between nuclear spins in partially aligned samples offer unique insights into biomacromolecular structure and dynamics. To fully benefit from the RDC data, accurate knowledge of the magnitude ( D (a)) and rhombicity ( R ) of the molecular alignment tensor, A, is important. An extended ...

journal_title：Journal of biomolecular NMR

authors： Bryce DL,Bax A

更新日期：2004-03-01 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：: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

authors： Shcherbakov AA,Hong M

更新日期：2018-05-01 00:00:00

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

authors： Hyberts SG,Wagner G

更新日期：2003-08-01 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：:Simulated neural networks are described which aid the assignment of protein NMR spectra. A network trained to recognize amino acid type from TOCSY data was trained on 148 assigned spin systems from E. coli acyl carrier proteins (ACPs) and tested on spin systems from spinach ACP, which has a 37% sequence homology with ...

journal_title：Journal of biomolecular NMR

authors： Hare BJ,Prestegard JH

更新日期：1994-01-01 00:00:00

abstract：:Human ATP-binding cassette, sub-family B, member 6 (ABCB6) is a mitochondrial ABC transporter, and presumably contributes to iron homeostasis. Aimed at understanding the structural basis for the conformational changes accompanying the substrate-transportation cycle, we have studied the C-terminal nucleotide-binding do...

journal_title：Journal of biomolecular NMR

authors： Kurashima-Ito K,Ikeya T,Senbongi H,Tochio H,Mikawa T,Shibata T,Ito Y

更新日期：2006-05-01 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：:Residual dipolar couplings provide complementary information to the nuclear Overhauser effect measurements that are traditionally used in biomolecular structure determination by NMR. In a de novo structure determination, however, lack of knowledge about the degree and orientation of molecular alignment complicates the...

journal_title：Journal of biomolecular NMR

authors： Habeck M,Nilges M,Rieping W

更新日期：2008-02-01 00:00:00

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

authors： Schanda P,Kupce E,Brutscher B

更新日期：2005-12-01 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：: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

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

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：: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

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

更新日期：2015-05-01 00:00:00

abstract：:15N-C alpha and 15N-C' J couplings were measured for the backbone of staphylococcal nuclease, uniformly enriched with 15N and 13C. It is found that the 1JC'N coupling is similar for beta-sheet, J = 14.8 +/- 0.5 and for alpha-helix, J = 14.8 +/- 0.4 but tends to be larger for the unstructured N- and C-terminal ends of ...

journal_title：Journal of biomolecular NMR

authors： Delaglio F,Torchia DA,Bax A

更新日期：1991-11-01 00:00:00

abstract：:We present heteronuclear three-dimensional gradient-NMR techniques for the resonanceassignment of exchangeable (-OH and -NH) protons in uniformly 13C isotopically enrichedoligosaccharides and for the measurement of 1H-1H nuclear Overhauser enhancementsinvolving these protons. These techniques are derived from conventi...

journal_title：Journal of biomolecular NMR

authors： Harris R,Rutherford TJ,Milton MJ,Homans SW

更新日期：1997-01-01 00:00:00

abstract：:Due to practical limitations in available 15N rf field strength, imperfections in 15N 180 degrees pulses arising from off-resonance effects can result in significant sensitivity loss, even if the chemical shift offset is relatively small. Indeed, in multi-dimensional NMR experiments optimized for protein backbone amid...

journal_title：Journal of biomolecular NMR

authors： Iwahara J,Clore GM

更新日期：2006-12-01 00:00:00

abstract：:Staphylococcus aureus hibernation promoting factor (SaHPF) is a 22,2 kDa protein which plays a crucial role in 100S Staphylococcus aureus ribosome formation during stress. SaHPF consists of N-terminal domain (NTD) that prevents proteins synthesis by binding to the 30S subunit at the P- and A-sites, connected through a...

journal_title：Journal of biomolecular NMR

authors： Usachev KS,Validov SZ,Khusainov IS,Varfolomeev AA,Klochkov VV,Aganov AV,Yusupov MM

更新日期：2019-05-01 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：:The hydrogen-deuterium exchange rates of the reduced and oxidized forms of Rhodobacter capsulatus cytochrome c2 were studied by 1H-15N homonuclear multiple quantum correlation spectroscopy. Minimal differences were observed for the N- and C-terminal helices on changing redox state suggesting that although these helice...

journal_title：Journal of biomolecular NMR

authors： Gooley PR,Zhao D,MacKenzie NE

更新日期：1991-07-01 00:00:00

abstract：:We discuss the optimum experimental conditions to obtain assignment spectra for solid proteins at magic-angle spinning (MAS) frequencies around 100 kHz. We present a systematic examination of the MAS dependence of the amide proton T 2' times and a site-specific comparison of T 2' at 93 kHz versus 60 kHz MAS frequency....

journal_title：Journal of biomolecular NMR

authors： Penzel S,Smith AA,Agarwal V,Hunkeler A,Org ML,Samoson A,Böckmann A,Ernst M,Meier BH

更新日期：2015-10-01 00:00:00

abstract：:The Biological Magnetic Resonance Data Bank contains NMR chemical shift depositions for 132 RNAs and RNA-containing complexes. We have analyzed the (1)H NMR chemical shifts reported for non-exchangeable protons of residues that reside within A-form helical regions of these RNAs. The analysis focused on the central bas...

journal_title：Journal of biomolecular NMR

authors： Barton S,Heng X,Johnson BA,Summers MF

更新日期：2013-01-01 00:00:00

abstract：:We report the determination of the global fold of human ubiquitin using protein backbone NMR residual dipolar coupling and long-range nuclear Overhauser effect (NOE) data as conformational restraints. Specifically, by use of a maximum of three backbone residual dipolar couplings per residue (Ni-H N i, Ni-C'(i-1), H N ...

journal_title：Journal of biomolecular NMR

authors： Giesen AW,Homans SW,Brown JM

更新日期：2003-01-01 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