Selective 1H- 13C NMR spectroscopy of methyl groups in residually protonated samples of large proteins.

abstract：:Simultaneous data acquisition in time-sharing (TS) multi-dimensional NMR experiments has been shown an effective means to reduce experimental time, and thus to accelerate structure determination of proteins. This has been accomplished by spin evolution time-sharing of the X and Y heteronuclei, such as (15)N and (13)C,...

journal_title：Journal of biomolecular NMR

authors： Xia Y,Yee A,Arrowsmith CH,Gao X

更新日期：2003-11-01 00:00:00

abstract：:Backbone assignments for the isolated α-subunit of Salmonella typhimurium tryptophan synthase (TS) are reported based on triple resonance solution-state NMR experiments on a uniformly 2H,13C,15N-labeled sample. From the backbone chemical shifts, secondary structure and random coil index order parameters (RCI-S2) are p...

journal_title：Journal of biomolecular NMR

authors： Sakhrani VV,Hilario E,Caulkins BG,Hatcher-Skeers ME,Fan L,Dunn MF,Mueller LJ

更新日期：2020-07-01 00:00:00

abstract：:Protein structure determination of low affinity complexes of interacting macromolecules is often hampered by a lack of observable NOEs between the binding partners. Covalent linkage offers a way to shift the equilibrium of the interaction partners to the bound state. Here we show that a single-chain protein containing...

journal_title：Journal of biomolecular NMR

authors： Freund C,Kühne R,Park S,Thiemke K,Reinherz EL,Wagner G

更新日期：2003-10-01 00:00:00

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：: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：:In this work, we show how the water flip-back approach that is widely employed in solution-state NMR can be adapted to proton-detected MAS solid-state NMR of highly deuterated proteins. The scheme allows to enhance the sensitivity of the experiment by decreasing the recovery time of the proton longitudinal magnetizati...

journal_title：Journal of biomolecular NMR

authors： Chevelkov V,Xiang S,Giller K,Becker S,Lange A,Reif B

更新日期：2015-02-01 00:00:00

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

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

abstract：:Structural knowledge about proteins is mainly derived from values of observables, measurable in NMR spectroscopic or X-ray diffraction experiments, i.e. absorbed or scattered intensities, through theoretically derived relationships between structural quantities such as atom positions or torsional angles on the one han...

journal_title：Journal of biomolecular NMR

authors： Steiner D,Allison JR,Eichenberger AP,van Gunsteren WF

更新日期：2012-07-01 00:00:00

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

authors： Feng L,Lee HS,Prestegard JH

更新日期：2007-07-01 00:00:00

abstract：:A comparison is made of the consequences of using time-averaged and conventional vicinal (3)J-coupling restraints in molecular dynamics refinement of an adenosine nucleoside model system. The target values for the restraints are derived from a 3-ns unrestrained molecular dynamics simulation. A comparison of the result...

journal_title：Journal of biomolecular NMR

authors： Pearlman DA

更新日期：1994-03-01 00:00:00

abstract：:Segmental isotopic labeling can facilitate NMR studies of large proteins, multi-domain proteins, and proteins with repetitive sequences by alleviating NMR signal overlaps. Segmental isotopic labeling also allows us to investigate an individual domain in the context of a full-length protein by NMR. Several established ...

journal_title：Journal of biomolecular NMR

authors： Mikula KM,Krumwiede L,Plückthun A,Iwaï H

更新日期：2018-08-01 00:00:00

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

authors： Merkley N,Shaw GS

更新日期：2003-06-01 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：: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：:We present a computational method for finding optimal labeling patterns for the backbone assignment of membrane proteins and other large proteins that cannot be assigned by conventional strategies. Following the approach of Kainosho and Tsuji (Biochemistry 21:6273-6279 (1982)), types of amino acids are labeled with (1...

journal_title：Journal of biomolecular NMR

authors： Hefke F,Bagaria A,Reckel S,Ullrich SJ,Dötsch V,Glaubitz C,Güntert P

更新日期：2011-02-01 00:00:00

abstract：:Pulsed field gradients were incorporated into the HCACO experiment for acquiring spectra on isotopically enriched protein samples dissolved in H2O. Excellent water suppression and spectral quality were achieved using the modified pulse sequence (gd-HCACO), as demonstrated for a 13C-/15N-labeled sample of the SH2 domai...

journal_title：Journal of biomolecular NMR

authors： Zhang W,Gmeiner WH

更新日期：1996-05-01 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：:Understanding of the molecular mechanisms of protein function requires detailed insight into the conformational landscape accessible to the protein. Conformational changes can be crucial for biological processes, such as ligand binding, protein folding, and catalysis. NMR spectroscopy is exquisitely sensitive to such ...

journal_title：Journal of biomolecular NMR

authors： Chatterjee SD,Ubbink M,van Ingen H

更新日期：2018-06-01 00:00:00

abstract：:Detection of (15)N in multidimensional NMR experiments of proteins has sparsely been utilized because of the low gyromagnetic ratio (γ) of nitrogen and the presumed low sensitivity of such experiments. Here we show that selecting the TROSY components of proton-attached (15)N nuclei (TROSY (15)NH) yields high quality s...

journal_title：Journal of biomolecular NMR

authors： Takeuchi K,Arthanari H,Shimada I,Wagner G

更新日期：2015-12-01 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：: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：:The (1)H, (13)C and (15)N NMR resonances of the backbone of serine protease PB92 have been assigned. This 269-residue protein is one of the largest monomeric proteins assigned so far. The amount and quality of information available suggest that even larger proteins could be assigned with present methods. Measured chem...

journal_title：Journal of biomolecular NMR

authors： Fogh RH,Schipper D,Boelens R,Kaptein R

更新日期：1994-01-01 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 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：: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：: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：:Temperature coefficients have been measured for backbone amide (1)H and (15)N nuclei in the B1 domain of protein G (GB1), using temperatures in the range 283-313 K, and pH values from 2.0 to 9.0. Many nuclei display pH-dependent coefficients, which were fitted to one or two pK(a) values. (1)H coefficients showed the e...

journal_title：Journal of biomolecular NMR

authors： Tomlinson JH,Williamson MP

更新日期：2012-01-01 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：:The discovery of the TROSY effect (Pervushin et al. in Proc Natl Acad Sci USA 94:12366-12371, 1997) for reducing transverse relaxation and line sharpening through selecting pathways in which dipole-dipole and CSA Hamiltonians partially cancel each other had a tremendous impact on solution NMR studies of macromolecules...

journal_title：Journal of biomolecular NMR

authors： Takeuchi K,Arthanari H,Wagner G

更新日期：2016-12-01 00:00:00