NMR line shape analysis of a multi-state ligand binding mechanism in chitosanase.

abstract：:Calculated coupling constants (3JHNH alpha, 1JC alpha H alpha, 2JC'H alpha, 1JC alpha N and 2JC alpha N) from our accompanying paper [Edison, A.S. et al. (1994) J. Biomol. NMR, 4, 519-542] have been used to generate error surfaces that can provide estimates of the phi and psi angles in proteins. We have used experimen...

journal_title：Journal of biomolecular NMR

authors： Edison AS,Weinhold F,Westler WM,Markley JL

更新日期：1994-07-01 00:00:00

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

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

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

authors： Nanzer AP,van Gunsteren WF,Torda AE

更新日期：1995-11-01 00:00:00

abstract：:Recently we have shown that HMQC spectra of protonated methyl groups in high molecular weight, highly deuterated proteins have large enhancements in sensitivity and resolution relative to HSQC-generated data sets. These enhancements derive from a TROSY effect in which complete cancellation of intra-methyl (1)H-(1)H an...

journal_title：Journal of biomolecular NMR

authors： Tugarinov V,Kay LE

更新日期：2004-02-01 00:00:00

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

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

更新日期：1991-07-01 00:00:00

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

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

更新日期：2007-05-01 00:00:00

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

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

abstract：:We describe a novel method for the robust, rapid, and reliable determination of J couplings in multi-dimensional NMR coupling data, including small couplings from larger proteins. The method, "High-resolution Iterative Frequency Identification of Couplings" (HIFI-C) is an extension of the adaptive and intelligent data...

journal_title：Journal of biomolecular NMR

authors： Cornilescu G,Bahrami A,Tonelli M,Markley JL,Eghbalnia HR

更新日期：2007-08-01 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：:For the understanding of cellular processes the molecular structure of biomolecules has to be accurately determined. Initial models can be significantly improved by structure refinement techniques. Here, we present the refinement methods and analysis techniques implemented in the GROMOS software for biomolecular simul...

journal_title：Journal of biomolecular NMR

authors： Schmid N,Allison JR,Dolenc J,Eichenberger AP,Kunz AP,van Gunsteren WF

更新日期：2011-11-01 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：: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：: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

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

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

authors： Schubert M,Oschkinat H,Schmieder P

更新日期：2001-08-01 00:00:00

abstract：:TROSY-based triple resonance experiments are essential for protein backbone assignment of large biomolecular systems by solution NMR spectroscopy. In a survey of the current Bruker pulse sequence library for TROSY-based experiments we found that several sequences were plagued by artifacts that affect spectral quality ...

journal_title：Journal of biomolecular NMR

authors： Xia Y,Rossi P,Tonelli M,Huang C,Kalodimos CG,Veglia G

更新日期：2017-09-01 00:00:00

abstract：:One-dimensional transient NOE build-up curves were measured for the synthetic disaccharide alpha-D-Fuc-(1-->4)-beta-D-GlcNAc 1 utilizing Gaussian shaped pulses. Simulated build-up curves from Metropolis Monte Carlo simulations were compared to the experimental data. Disaccharide 1 is structurally related to methyl bet...

journal_title：Journal of biomolecular NMR

authors： Weimar T,Meyer B,Peters T

更新日期：1993-07-01 00:00:00

abstract：:G protein-coupled receptors (GPCRs) are transmembrane signal transducers which regulate many key physiological process. Since their discovery, their analysis has been limited by difficulties in obtaining sufficient amounts of the receptors in high-quality, functional form from heterologous expression hosts. Albeit hig...

journal_title：Journal of biomolecular NMR

authors： Abiko LA,Rogowski M,Gautier A,Schertler G,Grzesiek S

更新日期：2021-01-27 00:00:00

abstract：:NMR spectra of ubiquitin in the presence of bicelles at a concentration of 32% w/v have been recorded at 700 MHz under sample spinning conditions at the magic angle (54.7 degrees ) and at an angle of 45.5 degrees . At the magic angle, the 1H-15N HSQC spectrum of ubiquitin in bicelles is virtually indistinguishable fro...

journal_title：Journal of biomolecular NMR

authors： Lancelot N,Elbayed K,Piotto M

更新日期：2005-11-01 00:00:00

abstract：:While NMR studies of proteins typically aim at structure, dynamics or interactions, resonance assignments represent in almost all cases the initial step of the analysis. With increasing complexity of the NMR spectra, for example due to decreasing extent of ordered structure, this task often becomes both difficult and ...

journal_title：Journal of biomolecular NMR

authors： Zawadzka-Kazimierczuk A,Koźmiński W,Billeter M

更新日期：2012-09-01 00:00:00

abstract：:High-pressure NMR spectroscopy has emerged as a complementary approach for investigating various structural and thermodynamic properties of macromolecules. Noticeably absent from the array of experimental restraints that have been employed to characterize protein structures at high hydrostatic pressure is the residual...

journal_title：Journal of biomolecular NMR

authors： Fu Y,Wand AJ

更新日期：2013-08-01 00:00:00

abstract：:New nuclear magnetic resonance (NMR) methods are described for the measurement of cross-correlation rates of zero- and double-quantum coherences involving two nitrogen nuclei belonging to successive amino acids in proteins and peptides. Rates due to the concerted fluctuations of two NH(N) dipole-dipole interactions an...

journal_title：Journal of biomolecular NMR

authors： Pelupessy P,Ravindranathan S,Bodenhausen G

更新日期：2003-04-01 00:00:00

abstract：:Methyl (13)CHD(2) isotopomers of all methyl-containing amino-acids can be observed in residually protonated samples of large proteins obtained from [U-(13)C,(1)H]-glucose/D(2)O-based bacterial media, with sensitivity sufficient for a number of NMR applications. Selective detection of some subsets of methyl groups (Ala...

journal_title：Journal of biomolecular NMR

authors： Guo C,Tugarinov V

更新日期：2010-02-01 00:00:00

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

authors： Lange OF

更新日期：2014-07-01 00:00:00

abstract：:The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs runni...

journal_title：Journal of biomolecular NMR

authors： Delaglio F,Grzesiek S,Vuister GW,Zhu G,Pfeifer J,Bax A

更新日期：1995-11-01 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：: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

authors： Petros AM,Neri P,Fesik SW

更新日期：1992-01-01 00:00:00

abstract：:Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion NMR experiments are extremely powerful for characterizing millisecond time-scale conformational exchange processes in biomolecules. A large number of such CPMG experiments have now emerged for measuring protein backbone chemical shifts of sparsely populated (>0.5%...

journal_title：Journal of biomolecular NMR

authors： Vallurupalli P,Hansen DF,Lundström P,Kay LE

更新日期：2009-09-01 00:00:00

abstract：:We recently engineered encodable lanthanide binding tags (LBTs) into proteins and demonstrated their applicability in Nuclear Magnetic Resonance (NMR) spectroscopy, X-ray crystallography and luminescence studies. Here, we engineered two-loop-LBTs into the model protein interleukin-1β (IL1β) and measured (1)H, (15)N-ps...

journal_title：Journal of biomolecular NMR

authors： Barthelmes D,Gränz M,Barthelmes K,Allen KN,Imperiali B,Prisner T,Schwalbe H

更新日期：2015-11-01 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：:Four-dimensional NMR spectroscopy can be speeded up by a large factor by a projection-reconstruction technique related to that used in X-ray tomography. The limited amount of information recorded in a few suitably-tilted projection planes suffices to recreate the entire four-dimensional spectrum. The method is demonst...

journal_title：Journal of biomolecular NMR

authors： Kupce E,Freeman R

更新日期：2004-04-01 00:00:00