Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy.

abstract：:We describe a new labeling method that allows for full protonation at the backbone Hα position, maintaining protein side chains with a high level of deuteration. We refer to the method as alpha proton exchange by transamination (α-PET) since it relies on transaminase activity demonstrated here using Escherichia coli e...

journal_title：Journal of biomolecular NMR

authors： Movellan KT,Najbauer EE,Pratihar S,Salvi M,Giller K,Becker S,Andreas LB

更新日期：2019-02-01 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：:In magic angle spinning solid state NMR experiments the potential of heteronuclear (1)H decoupling employing a continuous train of adiabatic inversion pulses has been assessed via numerical simulations and experimental measurements. It is shown that, with a (1)H RF field strength of approximately 100 kHz that is typic...

journal_title：Journal of biomolecular NMR

authors： Leppert J,Ohlenschläger O,Görlach M,Ramachandran R

更新日期：2004-07-01 00:00:00

abstract：:A simple constant-time 3D heteronuclear NMR pulse sequence has been developed to quantitatively determine the heteronuclear three-bond couplings 3J(HN,C') and 3J(H beta,C') in uniformly 13C-enriched proteins. The protocols for measuring accurate coupling constants are based on 1H,13C-heteronuclear relayed E.COSY [Schm...

journal_title：Journal of biomolecular NMR

authors： Schmidt JM,Löhr F,Rüterjans H

更新日期：1996-03-01 00:00:00

abstract：:In order to understand the role of the glycans in glycoproteins in solution, structural information obtained by NMR spectroscopy is obviously required. However, the assignment of the NMR signals from the glycans in larger glycoproteins is still difficult, mainly due to the lack of appropriate methods for the assignmen...

journal_title：Journal of biomolecular NMR

authors： Yamaguchi Y,Takizawa T,Kato K,Arata Y,Shimada I

更新日期：2000-12-01 00:00:00

abstract：:The use of pulsed field gradients in multiple-pulse NMR experiments has many advantages, including the possibility of obtaining excellent water suppression without the need for selective presaturation. In such gradient experiments the water magnetization is dephased deliberately; exchange between the saturated protons...

journal_title：Journal of biomolecular NMR

authors： Stonehouse J,Clowes RT,Shaw GL,Keeler J,Laue ED

更新日期：1995-04-01 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：: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：:The inclusion of explicit solvent water in molecular dynamics refinement of NMR structures ought to provide the most physically meaningful accounting for the effects of solvent on structure, but is computationally expensive. In order to evaluate the validity of commonly used vacuum refinements and of recently develope...

journal_title：Journal of biomolecular NMR

authors： Xia B,Tsui V,Case DA,Dyson HJ,Wright PE

更新日期：2002-04-01 00:00:00

abstract：:Residual dipolar couplings (RDC) between nuclear spins in partially aligned samples offer unique insights into biomacromolecular structure and dynamics. To fully benefit from the RDC data, accurate knowledge of the magnitude ( D (a)) and rhombicity ( R ) of the molecular alignment tensor, A, is important. An extended ...

journal_title：Journal of biomolecular NMR

authors： Bryce DL,Bax A

更新日期：2004-03-01 00:00:00

abstract：:Dynamics of large-amplitude conformational motions in proteins are complex and less understood, although these processes are intimately associated with structure, folding, stability, and function of proteins. Here, we use a large set of spectra obtained by cross-relaxation suppressed exchange NMR spectroscopy (EXSY) t...

journal_title：Journal of biomolecular NMR

authors： Rao DK,Bhuyan AK

更新日期：2007-11-01 00:00:00

abstract：:An 'isotopomer-selected NOE' (ISNOE) method for the unequivocal identification of mutually hydrogen-bond-linked hydroxyl groups is described. It relies on the fact that the OH group's signal patterns obtained for a partially deuterated sample originate from both isotopomers of the 'partner' hydroxyl, whereas a NOE for...

journal_title：Journal of biomolecular NMR

authors： Dabrowski J,Grosskurth H,Baust C,Nifant'ev NE

更新日期：1998-07-01 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：: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：: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：:Two-dimensional versions of HNCA and HNCO experiments are described, which provide essentially the same information as the 3D sequence. A multiple-quantum coherence involving either 15N and 13C alpha or 15N and 13CO is created. One of the two frequencies is given by the middle point between the two cross peaks (zero- ...

journal_title：Journal of biomolecular NMR

authors： Simorre JP,Brutscher B,Caffrey MS,Marion D

更新日期：1994-05-01 00:00:00

abstract：:Insights into the structure and dynamics of large biological systems has been greatly improved by two concurrent NMR approaches: the application of transverse relaxation-optimized spectroscopy (TROSY) techniques in multi-dimensional NMR, especially the methyl-TROSY, and the resurgence of 19F NMR using trifluoromethyl ...

journal_title：Journal of biomolecular NMR

authors： Klein BA,Sykes BD

更新日期：2019-11-01 00:00:00

abstract：:The ATP binding cassette transporter TAPL translocates cytosolic peptides into the lumen of lysosomes driven by the hydrolysis of ATP. Functionally, this transporter can be divided into coreTAPL, comprising the transport function, and an additional N-terminal transmembrane domain called TMD0, which is essential for ly...

journal_title：Journal of biomolecular NMR

authors： Tumulka F,Roos C,Löhr F,Bock C,Bernhard F,Dötsch V,Abele R

更新日期：2013-10-01 00:00:00

abstract：:New base-type-edited transverse-relaxation optimized CT-HCN(C) experiments are presented that yield intra-base and sugar-to-base correlations for 13C-15N labeled RNA. High spectral resolution in the 13C and 15N dimensions is achieved by constant time (CT) frequency editing. A spectral editing filter applied during the...

journal_title：Journal of biomolecular NMR

authors： Van Melckebeke H,Pardi A,Boisbouvier J,Simorre JP,Brutscher B

更新日期：2005-08-01 00:00:00

abstract：:Sensitivity and resolution together determine the quality of NMR spectra in biological solids. For high-resolution structure determination with solid-state NMR, proton-detection emerged as an attractive strategy in the last few years. Recent progress in probe technology has extended the range of available MAS frequenc...

journal_title：Journal of biomolecular NMR

authors： Xue K,Sarkar R,Tosner Z,Lalli D,Motz C,Koch B,Pintacuda G,Reif B

更新日期：2019-11-01 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：: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 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：:Due to practical limitations in available 15N rf field strength, imperfections in 15N 180 degrees pulses arising from off-resonance effects can result in significant sensitivity loss, even if the chemical shift offset is relatively small. Indeed, in multi-dimensional NMR experiments optimized for protein backbone amid...

journal_title：Journal of biomolecular NMR

authors： Iwahara J,Clore GM

更新日期：2006-12-01 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：:This paper describes the use of single transition-to-single transition polarization transfer (ST2-PT) in transverse relaxation-optimized spectroscopy (TROSY), where it affords a [Formula: see text] sensitivity enhancement for kinetically stable amide 15N-1H groups in proteins. Additional, conventional improvements of ...

journal_title：Journal of biomolecular NMR

authors： Pervushin KV,Wider G,Wüthrich K

更新日期：1998-08-01 00:00:00

abstract：:An improved version of the three-dimensional HCCH-COSY NMR experiment is described that correlates the resonances of geminal and vicinal proton pairs with the chemical shift of the 13C nucleus attached to one of the protons. The experiment uses constant-time evolution of transverse 13C magnetization which optimizes tr...

journal_title：Journal of biomolecular NMR

authors： Ikura M,Kay LE,Bax A

更新日期：1991-09-01 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：:NMR spectroscopy is uniquely suited for atomic resolution studies of biomolecules such as proteins, nucleic acids and metabolites, since detailed information on structure and dynamics are encoded in positions and line shapes of peaks in NMR spectra. Unfortunately, accurate determination of these parameters is often co...

journal_title：Journal of biomolecular NMR

authors： Niklasson M,Otten R,Ahlner A,Andresen C,Schlagnitweit J,Petzold K,Lundström P

更新日期：2017-10-01 00:00:00

abstract：:A major difficulty in determining the structure of an oligomeric protein by NMR is the problem of distinguishing inter- from intraprotomer NOEs. In order to address this issue in studies of the 27 kD compact trimeric domain of the MHC class II-associated invariant chain, we compared the 13C NOESY-HSQC spectrum of a un...

journal_title：Journal of biomolecular NMR

authors： Jasanoff A

更新日期：1998-08-01 00:00:00