نتایج جستجو برای: 15n and 13c

تعداد نتایج: 16830084  

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1997
K Pervushin R Riek G Wider K Wüthrich

Fast transverse relaxation of 1H, 15N, and 13C by dipole-dipole coupling (DD) and chemical shift anisotropy (CSA) modulated by rotational molecular motions has a dominant impact on the size limit for biomacromolecular structures that can be studied by NMR spectroscopy in solution. Transverse relaxation-optimized spectroscopy (TROSY) is an approach for suppression of transverse relaxation in mul...

Journal: :Physical chemistry chemical physics : PCCP 2008
Benjamin J Wylie Lindsay J Sperling Chad M Rienstra

Here we examine the effect of magic-angle spinning (MAS) rate upon lineshape and observed peak position for backbone carbonyl (C') peaks in NMR spectra of uniformly-(13)C,15N-labeled (U-(13)C,15N) solid proteins. 2D N-C' spectra of U-(13)C,15N microcrystalline protein GB1 were acquired at six MAS rates, and the site-resolved C' lineshapes were analyzed by numerical simulations and comparison to...

2014
Takanori Komatsu Risa Ohishi Amiu Shino Kinya Akashi Jun Kikuchi

In the present study, we applied nuclear magnetic resonance (NMR), as well as near-infrared (NIR) spectroscopy, to Jatropha curcas to fulfill two objectives: (1) to qualitatively examine the seeds stored at different conditions, and (2) to monitor the metabolism of J. curcas during its initial growth stage under stable-isotope-labeling condition (until 15 days after seeding). NIR spectra could ...

Journal: :Journal of biomolecular NMR 1997
F J Moy M R Pisano P K Chanda C Urbano L M Killar M L Sung R Powers

Fibroblast collagenase (MMP-1), a 169-residue protein with a molecular mass of 18.7 kDa, is a matrix metalloproteinase which has been associated with pathologies such as arthritis and cancer. The assignments of the 1H, 15N, 13CO and 13C resonances, determination of the secondary structure and analysis of 15N relaxation data of the inhibitor-free catalytic fragment of recombinant human fibroblas...

Journal: :Science 1997
N Tjandra A Bax

In isotropic solution, internuclear dipolar couplings average to zero as a result of rotational diffusion. By dissolving macromolecules in a dilute aqueous nematic discotic liquid-crystalline medium containing widely spaced magnetically oriented particles, a tunable degree of solute alignment with the magnetic field can be created while retaining the high resolution and sensitivity of the regul...

Journal: :Isotopes in environmental and health studies 2008
Jorge E Spangenberg Irenaus Matuschik Stephanie Jacomet Joerg Schibler

The molecular and isotopic chemistry of organic residues from archaeological potsherds was used to obtain further insight into the dietary trends and economies at the Constance lake-shore Neolithic settlements. The archaeological organic residues from the Early Late Neolithic (3922-3902 BC) site Hornstaad-Hornle IA/Germany are, at present, the oldest archaeological samples analysed at the Insti...

2017
Ulrich Weininger

Experimental studies on protein dynamics at atomic resolution by NMR-spectroscopy in solution require isolated 1H-X spin pairs. This is the default scenario in standard 1H-15N backbone experiments. Side chain dynamic experiments, which allow to study specific local processes like proton-transfer, or tautomerization, require isolated 1H-13C sites which must be produced by site-selective 13C labe...

Journal: :Diabetes 2001
B Ahlman M Charlton A Fu C Berg P O'Brien K S Nair

Insulin's effect on the synthesis of liver proteins remains to be fully defined. Previous studies using various surrogate measures of amino acyl-tRNA have reported variable results of insulin's effect on liver protein synthesis. We determined the effect of insulin with or without amino acid supplementation on the synthesis rates of liver proteins (tissue, albumin, and fibrinogen) using L-[1-13C...

Journal: :Journal of the American Chemical Society 2006
Keith L Constantine Malcolm E Davis William J Metzler Luciano Mueller Brian L Claus

Given the three-dimensional (3D) structure of a protein, the binding pose of a ligand can be determined using distance restraints derived from assigned intra-ligand and protein-ligand nuclear Overhauser effects (NOEs). A primary limitation of this approach is the need for resonance assignments of the ligand-bound protein. We have developed an approach that utilizes data from 3D 13C-edited, 13C/...

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