Comparison of fast backbone dynamics at amide nitrogen and carbonyl sites in dematin headpiece C-terminal domain and its S74E mutant.

abstract：:A new homonuclear Hartmann-Hahn-type mixing scheme is introduced that effects coherence transfer between resonances in two separated frequency bands. The mixing scheme relies on the irradiation of two-band selective shaped pulses that are expanded in an MLEV-16 supercycle. Similar to heteronuclear Hartmann-Hahn experi...

journal_title：Journal of biomolecular NMR

authors： Carlomagno T,Maurer M,Sattler M,Schwendinger MG,Glaser SJ,Griesinger C

更新日期：1996-09-01 00:00:00

abstract：:Accessible surface area (ASA) is the surface area of an atom, amino acid or biomolecule that is exposed to solvent. The calculation of a molecule's ASA requires three-dimensional coordinate data and the use of a "rolling ball" algorithm to both define and calculate the ASA. For polymers such as proteins, the ASA for i...

journal_title：Journal of biomolecular NMR

authors： Hafsa NE,Arndt D,Wishart DS

更新日期：2015-07-01 00:00:00

abstract：:As part of efforts to develop improved methods for NMR protein sample preparation and structure determination, the Northeast Structural Genomics Consortium (NESG) has implemented an NMR screening pipeline for protein target selection, construct optimization, and buffer optimization, incorporating efficient microscale ...

journal_title：Journal of biomolecular NMR

authors： Rossi P,Swapna GV,Huang YJ,Aramini JM,Anklin C,Conover K,Hamilton K,Xiao R,Acton TB,Ertekin A,Everett JK,Montelione GT

更新日期：2010-01-01 00:00:00

abstract：:A new method, a restrained Monte Carlo (rMC) calculation, is demonstrated for generating high-resolution structures of DNA oligonucleotides in solution from interproton distance restraints and bounds derived from complete relaxation matrix analysis of two-dimensional nuclear Overhauser effect (NOE) spectral peak inten...

journal_title：Journal of biomolecular NMR

authors： Ulyanov NB,Schmitz U,James TL

更新日期：1993-09-01 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：: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：: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：: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 new isotope labeling technique for peptide segments in a protein sample was recently established using the protein splicing element intein [Yamazaki et al. (1998) J. Am. Chem. Soc., 120, 5591-5592]. This method makes it possible to observe signals of a selected amino (N-) or carboxyl (C-) terminal region along a pep...

journal_title：Journal of biomolecular NMR

authors： Otomo T,Teruya K,Uegaki K,Yamazaki T,Kyogoku Y

更新日期：1999-06-01 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：:A simple spectroscopic filtering technique is presented that may aid the assignment of (13)C and (15)N resonances of methyl-containing amino-acids in solid-state magic-angle spinning (MAS) NMR. A filtering block that selects methyl resonances is introduced in two-dimensional (2D) (13)C-homonuclear and (15)N-(13)C hete...

journal_title：Journal of biomolecular NMR

authors： Jehle S,Hiller M,Rehbein K,Diehl A,Oschkinat H,van Rossum BJ

更新日期：2006-11-01 00:00:00

abstract：:Three methods for calculating nuclear magnetic resonance cross-relaxation rates from molecular dynamics simulations of small flexible molecules have been compared in terms of their ability to reproduce relaxation data obtained experimentally and to produce consistent descriptions of the system. The importance of the a...

journal_title：Journal of biomolecular NMR

authors： Feenstra KA,Peter C,Scheek RM,van Gunsteren WF,Mark AE

更新日期：2002-07-01 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：: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：: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：: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：:Scalar coupling correlations across hydrogen bonds with carbonyl groups as acceptors have been observed in a variety of proteins, but not in nucleic acids. Here we present a pulse scheme that allows such an observation and quantification of trans-hydrogen bond 3hJ(NC)' correlations in nucleic acid base pairs, between ...

journal_title：Journal of biomolecular NMR

authors： Dingley AJ,Masse JE,Feigon J,Grzesiek S

更新日期：2000-04-01 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：:The cryogenic temperatures at which dynamic nuclear polarization (DNP) solid-state NMR experiments need to be carried out cause line-broadening, an effect that is especially detrimental for crowded protein spectra. By increasing the magnetic field strength from 600 to 800 MHz, the resolution of DNP spectra of type III...

journal_title：Journal of biomolecular NMR

authors： Fricke P,Mance D,Chevelkov V,Giller K,Becker S,Baldus M,Lange A

更新日期：2016-08-01 00:00:00

abstract：:Although beta-lactoglobulin (beta-LG) has been studied extensively for more than 50 years, its physical properties in solution are not yet understood fully in terms of its three-dimensional (3D) structure. For example, despite a recent high-resolution crystal structure, it is still not clear why the two common variant...

journal_title：Journal of biomolecular NMR

authors： Uhrínová S,Uhrín D,Denton H,Smith M,Sawyer L,Barlow PN

更新日期：1998-07-01 00:00:00

abstract：:The human alpha 3-chain type VI collagen C-terminal Kunitz domain fragment (alpha 3(VI)) has been studied by two dimensional 1H-1H and 1H-13C NMR spectroscopy at 303 K. It is shown that the secondary structure of the protein is strikingly similar to that of BPTI, and a number of unusual H alpha chemical shifts, which ...

journal_title：Journal of biomolecular NMR

authors： Sørensen MD,Kristensen SM,Bjørn S,Norris K,Olsen O,Led JJ

更新日期：1996-12-01 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：: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：:It has been demonstrated that protein folds can be determined using appropriate computational protocols with NMR chemical shifts as the sole source of experimental restraints. While such approaches are very promising they still suffer from low convergence resulting in long computation times to achieve accurate results...

journal_title：Journal of biomolecular NMR

authors： Rasia RM,Lescop E,Palatnik JF,Boisbouvier J,Brutscher B

更新日期：2011-11-01 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：: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：: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：:This study presents the first application of the model-free analysis (MFA) (Meiler in J Am Chem Soc 123:6098-6107, 2001; Lakomek in J Biomol NMR 34:101-115, 2006) to methyl group RDCs measured in 13 different alignment media in order to describe their supra-tau (c) dynamics in ubiquitin. Our results indicate that meth...

journal_title：Journal of biomolecular NMR

authors： Farès C,Lakomek NA,Walter KF,Frank BT,Meiler J,Becker S,Griesinger C

更新日期：2009-09-01 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：:Lanthanide complexes based on the DOTA (1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid) cage are commonly used as phase contrast agents in magnetic resonance imaging, but can also be utilized in structural NMR applications due to their ability to induce either paramagnetic relaxation enhancement or a pseudoc...

journal_title：Journal of biomolecular NMR

authors： Strickland M,Schwieters CD,Göbl C,Opina AC,Strub MP,Swenson RE,Vasalatiy O,Tjandra N

更新日期：2016-10-01 00:00:00