Analytical optimization of active bandwidth and quality factor for TOCSY experiments in NMR spectroscopy.

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：: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

authors： Akasaka K,Naito A,Nakatani H

更新日期：1991-05-01 00:00:00

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

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

更新日期：1994-09-01 00:00:00

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

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

更新日期：1992-11-01 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：:Extensive resonance overlap exacerbates assignment of intrinsically disordered proteins (IDPs). This issue can be circumvented by utilizing (15)N, (13)C' and (1)H(N) spins, where the chemical shift dispersion is mainly dictated by the characteristics of consecutive amino acid residues. Especially (15)N and (13)C' spin...

journal_title：Journal of biomolecular NMR

authors： Mäntylahti S,Hellman M,Permi P

更新日期：2011-02-01 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 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：:Calmodulin is a two-domain protein which in solution can adopt a variety of conformations upon reorientation of its domains. The maximum occurrence (MO) of a set of calmodulin conformations that are representative of the overall conformational space possibly sampled by the protein, has been calculated from the paramag...

journal_title：Journal of biomolecular NMR

authors： Dasgupta S,Hu X,Keizers PH,Liu WM,Luchinat C,Nagulapalli M,Overhand M,Parigi G,Sgheri L,Ubbink M

更新日期：2011-11-01 00:00:00

abstract：:Solid-state NMR spectra of membrane proteins often show significant line broadening at cryogenic temperatures. Here we investigate the effects of several cryoprotectants to preserve the spectral resolution of lipid membranes and membrane peptides at temperatures down to ~200 K. Trehalose, glycerol, dimethylsulfoxide (...

journal_title：Journal of biomolecular NMR

authors： Lee M,Hong M

更新日期：2014-08-01 00:00:00

abstract：:Activated dynamics plays a central role in protein function, where transitions between distinct conformations often underlie the switching between active and inactive states. The characteristic time scales of these transitions typically fall in the microsecond to millisecond range, which is amenable to investigations ...

journal_title：Journal of biomolecular NMR

authors： Weininger U,Blissing AT,Hennig J,Ahlner A,Liu Z,Vogel HJ,Akke M,Lundström P

更新日期：2013-09-01 00:00:00

abstract：:Adiabatic pulses have been widely used for broadband decoupling and spin inversion at high magnetic fields. In this paper we propose adiabatic pulses and supercycles that can be used at high magnetic fields like 800 or 900 MHz to obtain broadband TOCSY sequences with C,C or H,H J-transfer. The new mixing sequences are...

journal_title：Journal of biomolecular NMR

authors： Peti W,Griesinger C,Bermel W

更新日期：2000-11-01 00:00:00

abstract：:Under the condition that the longitudinal relaxation time of spin I is shorter than the longitudinal relaxation time of spin S the steady-state magnetization in [S,I]-TROSY-type experiments can be enhanced by intermediate storage of a part of the steady-state magnetization of spin I on spin S with a pulse sequence ele...

journal_title：Journal of biomolecular NMR

authors： Riek R

更新日期：2001-10-01 00:00:00

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

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

更新日期：2008-09-01 00:00:00

abstract：:The unnatural duplex oligonucleotide alpha-d(CGCAATTCGC).beta-d(GCGTTAAGCG) was analyzed by high-resolution NMR methods. All of the exchangeable imino and nonexchangeable protons of the duplex were assigned. Detection of all 10 of the exchangeable imino protons confirms that a parallel, unsymmetrical duplex is formed....

journal_title：Journal of biomolecular NMR

authors： Gmeiner WH,Rayner B,Morvan F,Imbach JL,Lown JW

更新日期：1992-05-01 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：: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

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

更新日期：2008-03-01 00:00:00

abstract：:Complex mixtures are at the heart of biology, and biomacromolecules almost always exhibit their function in a mixture, e.g., the mode of action for a spider venom is typically dependent on a cocktail of compounds, not just the protein. Information about diseases is encoded in body fluids such as urine and plasma in th...

journal_title：Journal of biomolecular NMR

authors： Björnerås J,Botana A,Morris GA,Nilsson M

更新日期：2014-04-01 00:00:00

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

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

更新日期：1993-11-01 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：:Chitosan interaction with chitosanase was examined through analysis of spectral line shapes in the NMR HSQC titration experiments. We established that the substrate, chitosan hexamer, binds to the enzyme through the three-state induced-fit mechanism with fast formation of the encounter complex followed by slow isomeri...

journal_title：Journal of biomolecular NMR

authors： Shinya S,Ghinet MG,Brzezinski R,Furuita K,Kojima C,Shah S,Kovrigin EL,Fukamizo T

更新日期：2017-04-01 00:00:00

abstract：:Signal overlapping is a major bottleneck for protein NMR analysis. We propose a new method, stable-isotope-assisted parameter extraction (SiPex), to resolve overlapping signals by a combination of amino-acid selective isotope labeling (AASIL) and tensor decomposition. The basic idea of Sipex is that overlapping signal...

journal_title：Journal of biomolecular NMR

authors： Kasai T,Ono S,Koshiba S,Yamamoto M,Tanaka T,Ikeda S,Kigawa T

更新日期：2020-03-01 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：:An improved version of the three-dimensional HCCH-COSY NMR experiment is described that correlates the resonances of geminal and vicinal proton pairs with the chemical shift of the 13C nucleus attached to one of the protons. The experiment uses constant-time evolution of transverse 13C magnetization which optimizes tr...

journal_title：Journal of biomolecular NMR

authors： Ikura M,Kay LE,Bax A

更新日期：1991-09-01 00:00:00

abstract：:Two-dimensional versions of HNCA and HNCO experiments are described, which provide essentially the same information as the 3D sequence. A multiple-quantum coherence involving either 15N and 13C alpha or 15N and 13CO is created. One of the two frequencies is given by the middle point between the two cross peaks (zero- ...

journal_title：Journal of biomolecular NMR

authors： Simorre JP,Brutscher B,Caffrey MS,Marion D

更新日期：1994-05-01 00:00:00

abstract：:Although dynamic nuclear polarization (DNP) has dramatically enhanced solid-state NMR spectral sensitivities of many synthetic materials and some biological macromolecules, recent studies of membrane-protein DNP using exogenously doped paramagnetic radicals as polarizing agents have reported varied and sometimes surpr...

journal_title：Journal of biomolecular NMR

authors： Liao SY,Lee M,Wang T,Sergeyev IV,Hong M

更新日期：2016-03-01 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：: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：:Post-translationally modified proteins make up the majority of the proteome and establish, to a large part, the impressive level of functional diversity in higher, multi-cellular organisms. Most eukaryotic post-translational protein modifications (PTMs) denote reversible, covalent additions of small chemical entities ...

journal_title：Journal of biomolecular NMR

authors： Theillet FX,Smet-Nocca C,Liokatis S,Thongwichian R,Kosten J,Yoon MK,Kriwacki RW,Landrieu I,Lippens G,Selenko P

更新日期：2012-11-01 00:00:00

abstract：:Many regulatory RNAs undergo dynamic exchanges that are crucial for their biological functions and NMR spectroscopy is a versatile tool for monitoring dynamic motions of biomolecules. Meaningful information on biomolecular dynamics requires an accurate measurement of relaxation parameters such as longitudinal (R1) rat...

journal_title：Journal of biomolecular NMR

authors： Nam H,Becette O,LeBlanc RM,Oh D,Case DA,Dayie TK

更新日期：2020-07-01 00:00:00