Application of correlated residual dipolar couplings to the determination of the molecular alignment tensor magnitude of oriented proteins and nucleic acids.

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：: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：:Many nucleic acids and proteins require divalent metal ions such as Mg(2+) and Ca(2+) for folding and function. The lipophilic alignment media frequently used as membrane mimetics also bind these divalent metals. Here we demonstrate the use of (31)P NMR spectrum of a metal ion chelator (deoxycytidine diphosphate) to m...

journal_title：Journal of biomolecular NMR

authors： Kozlyuk N,Sengupta S,Lupták A,Martin RW

更新日期：2016-04-01 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 biological environment in which a protein performs its function is a crowded milieu containing millions of molecules that can potentially lead to a great many transient, non-specific interactions. NMR spectroscopy is especially well suited to study these weak molecular contacts. Here, non-specific interactions bet...

journal_title：Journal of biomolecular NMR

authors： Latham MP,Kay LE

更新日期：2013-03-01 00:00:00

abstract：:We present a computer algorithm for the automated assignment of polypeptide backbone and 13C beta resonances of a protein of known primary sequence. Input to the algorithm consists of cross peaks from several 3D NMR experiments: HNCA, HN(CA)CO, HN(CA)HA, HNCACB, COCAH, HCA(CO)N, HNCO, HN(CO)CA, HN(COCA)HA, and CBCA(CO...

journal_title：Journal of biomolecular NMR

authors： Lukin JA,Gove AP,Talukdar SN,Ho C

更新日期：1997-02-01 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：:A method is proposed to determine the conformational equilibrium of flexible polypeptides in solution, using the data provided by NMR spectroscopy and theoretical conformational calculations. The algorithm consists of the following three steps: (i) search of the conformational space in order to find conformations with...

journal_title：Journal of biomolecular NMR

authors： Groth M,Malicka J,Czaplewski C,Ołdziej S,Lankiewicz L,Wiczk W,Liwo A

更新日期：1999-12-01 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：:Although dynamic nuclear polarization (DNP) has dramatically enhanced solid-state NMR spectral sensitivities of many synthetic materials and some biological macromolecules, recent studies of membrane-protein DNP using exogenously doped paramagnetic radicals as polarizing agents have reported varied and sometimes surpr...

journal_title：Journal of biomolecular NMR

authors： Liao SY,Lee M,Wang T,Sergeyev IV,Hong M

更新日期：2016-03-01 00:00:00

abstract：:HNCO/HNCACO type correlation experiments are an alternative for assignment of backbone resonances in extensively deuterated proteins in the solid-state, given the fact that line widths on the order of 14-17 Hz are achieved in the carbonyl dimension without the need of high power decoupling. The achieved resolution dem...

journal_title：Journal of biomolecular NMR

authors： Linser R,Fink U,Reif B

更新日期：2010-05-01 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：: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：:Calmodulin is a two-domain protein which in solution can adopt a variety of conformations upon reorientation of its domains. The maximum occurrence (MO) of a set of calmodulin conformations that are representative of the overall conformational space possibly sampled by the protein, has been calculated from the paramag...

journal_title：Journal of biomolecular NMR

authors： Dasgupta S,Hu X,Keizers PH,Liu WM,Luchinat C,Nagulapalli M,Overhand M,Parigi G,Sgheri L,Ubbink M

更新日期：2011-11-01 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：: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：:An approach to the determination of the 2-(13)C' chemical shift (CS) tensor orientation in pyrimidine bases via heteronuclear MAS NMR spectroscopy is presented. Considering a dipolar coupled spin 1/2 network of the type S1-I-S2 consisting of directly bonded heteronuclear spins, we have carried out numerical simulation...

journal_title：Journal of biomolecular NMR

authors： Leppert J,Heise B,Ramachandran R

更新日期：2000-10-01 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：: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：:Relaxation measurements of side-chain 13CH2-groups of uniformly 13C labeled human ubiquitin were performed at 600 MHz and 800 MHz magnetic field strength at 30 degrees C. Dipole-dipole cross-correlated relaxation effects in T1 experiments were suppressed by the combination of radio-frequency pulses and pulsed field gr...

journal_title：Journal of biomolecular NMR

authors： Jin C,Prompers JJ,Brüschweiler R

更新日期：2003-07-01 00:00:00

abstract：:The chemical shifts of (13)C2 of adenosine residues of DNA were observed to experience a through-space or trans-hydrogen bond isotope effect as a result of deuterium substitution at the imino hydrogen site of base-paired thymidine residues. NMR measurements of several self-complementary DNA duplexes at natural abundan...

journal_title：Journal of biomolecular NMR

authors： Vakonakis I,LiWang AC

更新日期：2004-05-01 00:00:00

abstract：:The solution structure of the SH3 domain of human p56 Lck tyrosine kinase (Lck-SH3) has been determined by multidimensional heteronuclear NMR spectroscopy. The structure was calculated from a total of 935 experimental restraints comprising 785 distance restraints derived from 1017 assigned NOE cross peaks and 150 dihe...

journal_title：Journal of biomolecular NMR

authors： Hiroaki H,Klaus W,Senn H

更新日期：1996-09-01 00:00:00

abstract：:2D 15N-1H correlation spectra are ideal for measuring backbone amide populations to determine amide exchange protection factors in studies of protein folding or other structural features. Most protein NMR spectroscopists use HSQC, which has been shown to be generally superior to HMQC in both resolution and sensitivity...

journal_title：Journal of biomolecular NMR

authors： Davis JH

更新日期：1995-06-01 00:00:00

abstract：:The use of dipolar shifts as important constraints in refining molecular structure of paramagnetic metalloproteins by solution NMR is now well established. A crucial initial step in this procedure is the determination of the orientation. of the anisotropic paramagnetic susceptibility tensor in the molecular frame whic...

journal_title：Journal of biomolecular NMR

authors： Xia Z,Nguyen BD,La Mar GN

更新日期：2000-06-01 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：: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：:The NMR derived translational diffusion coefficients were performed on unlabeled and uniformly labeled 13C,15N human insulin in water, both in neat, with zinc ions only, and in pharmaceutical formulation, containing only m-cresol as phenolic ligand, glycerol and zinc ions. The results show the dominant role of the pH ...

journal_title：Journal of biomolecular NMR

authors： Sitkowski J,Bocian W,Bednarek E,Urbańczyk M,Koźmiński W,Borowicz P,Płucienniczak G,Łukasiewicz N,Sokołowska I,Kozerski L

更新日期：2018-06-01 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：: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：: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