推薦產品
一般說明
DLAM-LVproS-13CH3 has 13CH3 isotopomer precursors and contains protocol instructions for creation of isotopically-labeled proteins.
應用
For detection of long-range nOes or for the NMR study of large proteins
Methyl groups of leucine and valine precursors is labeled with 13CH3 isotopomer using DLAM-LVproS-13CH3 kit. Amino-acid selective labeling combined with modern NMR techniques is frequently employed as a useful tool for resolving resonance assignments. This kit has been tested with protein isotopic labeling in E. coli. DLAM-LVproS-13CH3 is used for optimal resonance dispersion of supramolecular protein structure in solution NMR spectroscopy.
包裝
This product may be available from bulk stock and can be packaged on demand. For information on pricing, availability and packaging, please contact Stable Isotopes Customer Service.
分析證明 (COA)
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Kit I Tong et al.
Journal of biomolecular NMR, 42(1), 59-67 (2008-09-03)
A simple and user-friendly method of labeling protein selectively with amino acids in vivo is introduced. This technique does not require the use of transaminase-deficient or auxotrophic strains. By manipulating the product feedback inhibitory loops of the E. coli amino
Stereospecific isotopic labeling of methyl groups for NMR spectroscopic studies of high-molecular-weight proteins.
Pierre Gans et al.
Angewandte Chemie (International ed. in English), 49(11), 1958-1962 (2010-02-17)
Rime Kerfah et al.
Current opinion in structural biology, 32, 113-122 (2015-04-17)
Nuclear magnetic resonance (NMR) spectroscopy is a uniquely powerful tool for studying the structure, dynamics and interactions of biomolecules at atomic resolution. In the past 15 years, the development of new isotopic labeling strategies has opened the possibility of exploiting
Silke Wiesner et al.
Current opinion in structural biology, 35, 60-67 (2015-09-26)
Intermolecular interactions are indispensible for biological function. Here we discuss how novel NMR techniques can provide unique insights into the assembly, dynamics and regulation of biomolecular complexes. We focus on applications that exploit the methyl TROSY effect and show that
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