Resolution-enhanced base-type-edited HCN experiment for RNA.

abstract：:The development of new protein labeling strategies, along with optimized experiments that exploit the label, have significantly impacted on the types of biochemical problems that can now be addressed by solution NMR spectroscopy. Here we describe how methyl labeling of key residues in a highly deuterated protein backg...

journal_title：Journal of biomolecular NMR

authors： Ruschak AM,Kay LE

更新日期：2010-01-01 00:00:00

abstract：:NifU-like proteins are a highly conserved protein that serves as the scaffold for assembly of Fe-S clusters. Chloroplastic NifU-like proteins have tandem NifU like domains, named domain I and domain II. Although the amino acid sequences of these domains are very similar to each other, the predicted functional region f...

journal_title：Journal of biomolecular NMR

authors： Kumeta H,Ogura K,Asayama M,Katoh S,Katoh E,Teshima K,Inagaki F

更新日期：2007-06-01 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

abstract：:Cytochrome c552 from the thermophilic bacterium Hydrogenobacter thermophilus is a typical c-type cytochrome which binds heme covalently via two thioether bonds between the two heme vinyl groups and two cysteine thiol groups in a CXXCH sequence motif. This protein was converted to a b-type cytochrome by substitution of...

journal_title：Journal of biomolecular NMR

authors： Tozawa K,Ferguson SJ,Redfield C,Smith LJ

更新日期：2015-06-01 00:00:00

abstract：:Resonance assignment is a prerequisite for almost any NMR-based study of proteins. It can be very challenging in some cases, however, due to the nature of the protein under investigation. This is the case with intrinsically disordered proteins, for example, whose NMR spectra suffer from low chemical shifts dispersion ...

journal_title：Journal of biomolecular NMR

authors： Piai A,Gonnelli L,Felli IC,Pierattelli R,Kazimierczuk K,Grudziąż K,Koźmiński W,Zawadzka-Kazimierczuk A

更新日期：2016-03-01 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：: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：:Residual dipolar couplings provide complementary information to the nuclear Overhauser effect measurements that are traditionally used in biomolecular structure determination by NMR. In a de novo structure determination, however, lack of knowledge about the degree and orientation of molecular alignment complicates the...

journal_title：Journal of biomolecular NMR

authors： Habeck M,Nilges M,Rieping W

更新日期：2008-02-01 00:00:00

abstract：:Characterization of the structure and dynamics of nucleic acids by NMR benefits significantly from position specifically labeled nucleotides. Here an E. coli strain deficient in the transketolase gene (tktA) and grown on glucose that is labeled at different carbon sites is shown to facilitate cost-effective and large ...

journal_title：Journal of biomolecular NMR

authors： Thakur CS,Luo Y,Chen B,Eldho NV,Dayie TK

更新日期：2012-02-01 00:00:00

abstract：:A computer program has been developed to accurately and automatically predict the 1H and 13C chemical shifts of unassigned proteins on the basis of sequence homology. The program (called SHIFTY) uses standard sequence alignment techniques to compare the sequence of an unassigned protein against the BioMagResBank--a pu...

journal_title：Journal of biomolecular NMR

authors： Wishart DS,Watson MS,Boyko RF,Sykes BD

更新日期：1997-12-01 00:00:00

abstract：:With the completion of genome sequencing projects, there are a large number of proteins for which we have little or no functional information. Since protein function is closely related to three-dimensional conformation, structural proteomics is one avenue where the role of proteins with unknown function can be investi...

journal_title：Journal of biomolecular NMR

authors： Julien O,Gignac I,Hutton A,Yee A,Arrowsmith CH,Gagné SM

更新日期：2006-06-01 00:00:00

abstract：:During the past three years it has become possible to compute ab initio the 13C, 15N and 19F NMR chemical shifts of many sites in native proteins. Chemical shifts are beginning to become a useful supplement to more established methods of solution structure determination, and may find utility in solid-state analysis as...

journal_title：Journal of biomolecular NMR

authors： Oldfield E

更新日期：1995-04-01 00:00:00

abstract：:Paramagnetic relaxation enhancement (PRE) measurements constitute a powerful approach for detecting both permanent and transient protein-protein interactions. Typical PRE experiments require an intrinsic or engineered paramagnetic site on one of the two interacting partners; while a second, diamagnetic binding partner...

journal_title：Journal of biomolecular NMR

authors： Olivieri C,Subrahmanian MV,Xia Y,Kim J,Porcelli F,Veglia G

更新日期：2018-03-01 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：:Defining the self-association state of a molecule in solution can be an important step in NMR-based structure determination. This is particularly true of peptides, where there can be a relatively small number of long-range interactions and misinterpretation of an intermolecular NOE as an intramolecular contact can hav...

journal_title：Journal of biomolecular NMR

authors： Yao S,Howlett GJ,Norton RS

更新日期：2000-02-01 00:00:00

abstract：:Two new techniques offering considerable improvements in the quality of 1H photo-CIDNP spectra of proteins are demonstrated. Both focus on the problem of progressive photo-degradation of the flavin dye used to generate polarization in exposed tryptophan, tyrosine and histidine side-chains. One approach uses rapid addi...

journal_title：Journal of biomolecular NMR

authors： Maeda K,Lyon CE,Lopez JJ,Cemazar M,Dobson CM,Hore PJ

更新日期：2000-03-01 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：: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：:Extensive spectral overlap presents a major problem for the NMR study of large RNAs. Here we present NMR techniques for resolution enhancement and spectral simplification of fully 13C labelled RNA. High-resolution 1H-13C correlation spectra are obtained by combining TROSY-type experiments with multiple-band-selective ...

journal_title：Journal of biomolecular NMR

authors： Brutscher B,Boisbouvier J,Kupce E,Tisné C,Dardel F,Marion D,Simorre JP

更新日期：2001-02-01 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：: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：: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：:Simple pulse schemes are presented for the measurement of methyl (13)C and (1)H CSA values from (1)H-(13)C dipole/(13)C CSA and (1)H-(13)C dipole/(1)H CSA cross-correlated relaxation. The methodology is applied to protein L and malate synthase G. Average (13)C CSA values are considerably smaller for Ile than Leu/Val (...

journal_title：Journal of biomolecular NMR

authors： Tugarinov V,Scheurer C,Brüschweiler R,Kay LE

更新日期：2004-12-01 00:00:00

abstract：:We report here the backbone 1HN, 15N, 13C alpha, 13CO, and 1H alpha NMR assignments for the catalytic domain of human fibroblast collagenase (HFC). Three independent assignment pathways (matching 1H, 13C alpha, and 13CO resonances) were used to establish sequential connections. The connections using 13C alpha resonanc...

journal_title：Journal of biomolecular NMR

authors： McCoy MA,Dellwo MJ,Schneider DM,Banks TM,Falvo J,Vavra KJ,Mathiowetz AM,Qoronfleh MW,Ciccarelli R,Cook ER,Pulvino TA,Wahl RC,Wang H

更新日期：1997-01-01 00:00:00

abstract：:The first reconstitution of an Fe2S2 ferredoxin with a diamagnetic prosthetic group was recently described [Kazanis et al. (1995) J. Am. Chem. Soc., 117, 6625-6626]. The replacement of the iron-sulfur cluster of the bacterial ferredoxin putidaredoxin (Pdx) by gallium (Ga3+) renders the protein diamagnetic and permits ...

journal_title：Journal of biomolecular NMR

authors： Kazanis S,Pochapsky TC

更新日期：1997-06-01 00:00:00

abstract：:Simulated neural networks are described which aid the assignment of protein NMR spectra. A network trained to recognize amino acid type from TOCSY data was trained on 148 assigned spin systems from E. coli acyl carrier proteins (ACPs) and tested on spin systems from spinach ACP, which has a 37% sequence homology with ...

journal_title：Journal of biomolecular NMR

authors： Hare BJ,Prestegard JH

更新日期：1994-01-01 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：:Considerable excitement has been aroused by recent new methods for speeding up multidimensional NMR experiments by radically modifying the normal time-domain sampling protocols. These new schemes include the filter diagonalization method, GFT-NMR, the single-scan two-dimensional technique, Hadamard spectroscopy, and a...

journal_title：Journal of biomolecular NMR

authors： Freeman R,Kupce E

更新日期：2003-10-01 00:00:00

abstract：:We present a time-shared 3D HSQC-NOESY experiment that enables one to simultaneously record (13)C- and (15)N-dispersed spectra in Ile, Leu and Val (ILV) methyl-labeled samples. This experiment is designed to delineate the two spectra which would otherwise overlap with one another when acquired together. These spectra ...

journal_title：Journal of biomolecular NMR

authors： Frueh DP,Leed A,Arthanari H,Koglin A,Walsh CT,Wagner G

更新日期：2009-11-01 00:00:00

abstract：:Protein-fusion constructs have been used with great success for enhancing expression of soluble recombinant protein and as tags for affinity purification. Unfortunately the most popular tags, such as GST and MBP, are large, which hinders direct NMR studies of the fusion proteins. Cleavage of the fusion proteins often ...

journal_title：Journal of biomolecular NMR

authors： Zhou P,Lugovskoy AA,Wagner G

更新日期：2001-05-01 00:00:00