On the calculation of ³Jαβ-coupling constants for side chains in proteins.

abstract：:19F solid-state NMR is an excellent approach for measuring long-range distances for structure determination and for studying molecular motion. For multi-fluorinated proteins, assignment of 19F chemical shifts has been traditionally carried out using mutagenesis. Here we show 2D 19F-13C correlation experiments that all...

journal_title：Journal of biomolecular NMR

authors： Shcherbakov AA,Roos M,Kwon B,Hong M

更新日期：2020-03-01 00:00:00

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

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

更新日期：1999-05-01 00:00:00

abstract：:The solution molecular structure of the four-iron ferredoxin (Fd) from the hyperthermophilic archaeon Thermococcus litoralis (Tl) has been investigated by 1H NMR spectroscopy. TOCSY and NOESY experiments in H2O, tailored to detect both weakly and strongly relaxed resonances, together with steady-state NOEs in both H2O...

journal_title：Journal of biomolecular NMR

authors： Donaire A,Zhou ZH,Adams MM,La Mar GN

更新日期：1996-01-01 00:00:00

abstract：:Recent advances in the field of in-cell NMR spectroscopy have made it possible to study proteins in the context of bacterial or mammalian cell extracts or even entire cells. As most mammalian cells are part of a multi-cellular complex, there is a need to develop novel NMR approaches enabling the study of proteins with...

journal_title：Journal of biomolecular NMR

authors： Damman R,Lucini Paioni A,Xenaki KT,Beltrán Hernández I,van Bergen En Henegouwen PMP,Baldus M

更新日期：2020-09-01 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：: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

authors： Celda B,Biamonti C,Arnau MJ,Tejero R,Montelione GT

更新日期：1995-02-01 00:00:00

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

authors： Sternberg U,Witter R

更新日期：2019-12-01 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：: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

authors： Saccenti E,Rosato A

更新日期：2008-04-01 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：:1H(i)-15 N(i)-13C'(i) dipole-chemical shift anisotropy (CSA) relaxation interference was quantified for the 13C,15N labeled zinc-finger protein qCRP2(LIM2). The cross-correlation rates obtained for residues located in the metal coordination sites of qCRP2(LIM2) show a high degree of correlation with the peptide plane ...

journal_title：Journal of biomolecular NMR

authors： Kloiber K,Schüler W,Konrat R

更新日期：2001-04-01 00:00:00

abstract：:Protein expression in E. coli grown in shaker flasks is a routine and pivotal tool in many research laboratories. To maximize protein yields, cells are normally induced in the middle of the linear growth phase, typically at an OD600 of ≤ 1 for cells grown in Luria-Bertani (LB) medium at 37 °C. We recently showed that ...

journal_title：Journal of biomolecular NMR

authors： Cai M,Huang Y,Craigie R,Clore GM

更新日期：2019-12-01 00:00:00

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

authors： Rennella E,Solyom Z,Brutscher B

更新日期：2014-11-01 00:00:00

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

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

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：:We demonstrate a novel methodology to disrupt the symmetry in the NMR spectra of homodimers. A paramagnetic probe is introduced sub-stoichiometrically to create an asymmetric system with the paramagnetic probe residing on only one monomer within the dimer. This creates sufficient magnetic anisotropy for resolution of ...

journal_title：Journal of biomolecular NMR

authors： Gaponenko V,Altieri AS,Li J,Byrd RA

更新日期：2002-10-01 00:00:00

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

authors： Ishima R,Louis JM,Torchia DA

更新日期：2001-10-01 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：:A new pulse sequence is presented for the measurement of relaxation dispersion profiles quantifying millisecond time-scale exchange dynamics of side-chain carbonyl groups in uniformly (13)C labeled proteins. The methodology has been tested using the 87-residue colicin E7 immunity protein, Im7, which is known to fold v...

journal_title：Journal of biomolecular NMR

authors： Hansen AL,Kay LE

更新日期：2011-08-01 00:00:00

abstract：:We demonstrate a novel sparse (13)C labelling approach for methylotrophic yeast P. pastoris expression system, towards solid-state NMR studies of eukaryotic membrane proteins. The labelling scheme was achieved by co-utilizing natural abundance methanol and specifically (13)C labelled glycerol as carbon sources in the ...

journal_title：Journal of biomolecular NMR

authors： Liu J,Liu C,Fan Y,Munro RA,Ladizhansky V,Brown LS,Wang S

更新日期：2016-05-01 00:00:00

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 dependenc...

journal_title：Journal of biomolecular NMR

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

更新日期：1999-01-01 00:00:00

abstract：:A new protocol is described for obtaining intraresidual and sequential correlations between carbonyl carbons and amide (1)H and (15)N resonances of amino acids. Frequency labeling of (13)CO spins occurs during a period required for the (13)C(α)-(15)N polarization transfer, leading to an optimized transfer efficiency. ...

journal_title：Journal of biomolecular NMR

authors： Löhr F,Rüterjans H

更新日期：1995-09-01 00:00:00

abstract：:The importance of protein chemical shift values for the determination of three-dimensional protein structure has increased in recent years because of the large databases of protein structures with assigned chemical shift data. These databases have allowed the investigation of the quantitative relationship between chem...

journal_title：Journal of biomolecular NMR

authors： Meiler J

更新日期：2003-05-01 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：:The icosahedral bacteriophage T7 is a 50 MDa double-stranded DNA (dsDNA) virus that infects Escherichia coli. Although there is substantial information on the physical and morphological properties of T7, structural information, based mostly on Raman spectroscopy and cryo-electron microscopy, is limited. Here, we apply...

journal_title：Journal of biomolecular NMR

authors： Abramov G,Goldbourt A

更新日期：2014-08-01 00:00:00

abstract：:RC-RNase is a pyrimidine-guanine sequence-specific ribonuclease and a sialic-acid-binding lectin purified from Rana catesbeiana (bullfrog) oocytes. This 111-amino acid protein exhibits cytotoxicity toward several tumor cell lines. In this paper we report the assignments of proton NMR resonances and the identification ...

journal_title：Journal of biomolecular NMR

authors： Chen C,Hom K,Huang RF,Chou PJ,Liao YD,Huang T

更新日期：1996-10-01 00:00:00

abstract：:PG-1 adopts a dimeric structure in dodecylphosphocholine (DPC) micelles, and a channel is formed by the association of several dimers but the molecular mechanisms of the membrane damage by non-α-helical peptides are still unknown. The formation of the PG-1 dimer is important for pore formation in the lipid bilayer, si...

journal_title：Journal of biomolecular NMR

authors： Usachev KS,Efimov SV,Kolosova OA,Filippov AV,Klochkov VV

更新日期：2015-04-01 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：:Two methods for the measurement of homonuclear 3J(HNH)alpha coupling constants are described. Both HSQC- and HMQC-type experiments employ 'quantitative J-correlation', in which the coupling constant of interest is obtained from the intensity ratio of cross peaks of two spectra. The first spectrum is acquired with 3J(H...

journal_title：Journal of biomolecular NMR

authors： Permi P,Kilpeläinen I,Annila A,Heikkinen S

更新日期：2000-01-01 00:00:00

abstract：:The efficiency of cell-free protein synthesis combined with combinatorial selective 15N-labelling provides a method for the rapid assignment of 15N-HSQC cross-peaks to the 19 different non-proline amino-acid types from five 15N-HSQC spectra. This strategy was explored with two different constructs of the C-terminal do...

journal_title：Journal of biomolecular NMR

authors： Wu PS,Ozawa K,Jergic S,Su XC,Dixon NE,Otting G

更新日期：2006-01-01 00:00:00