一般描述
SLAM-Aβ-13C3 kit which has 13C3 isotopomer precursor and contains protocol instructions for creation of isotopically-labeled proteins.
应用
For protein methyl group assignment by 13C isotope labeling of amino acid methyl groups separately or simultaneously.
SLAM-Aβ-13C3 is an optimized kit used to produce proteins with 13CH3 isotopomer on the alanine residue. This kit has been tested with protein isotopic labeling in E. coli. It is used for labeling methyl groups of different amino acids separately or simultaneously in proteins. This labeling technology can dramatically increase the size limit of proteins in solution NMR spectroscopy for structural analysis.
包装
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.
储存分类代码
11 - Combustible Solids
法规信息
新产品
Vipin Agarwal et al.
Journal of the American Chemical Society, 128(39), 12620-12621 (2006-09-28)
MAS solid-state NMR experiments applied to biological solids are still hampered by low sensitivity and resolution. In this work, we employ a deuteration scheme in which individual methyl groups are selectively protonated. This labeling scheme allows the acquisition of proton
César Fernández et al.
Current opinion in structural biology, 13(5), 570-580 (2003-10-22)
Transverse relaxation-optimized spectroscopy (TROSY), in combination with various isotope-labeling techniques, has opened avenues to study biomolecules with molecular masses of up to 1000000Da by solution NMR. Important recent applications of TROSY include the structure determination of membrane proteins in detergent
Rime Kerfah et al.
Journal of biomolecular NMR, 63(4), 389-402 (2015-11-15)
A new strategy for the NMR assignment of aliphatic side-chains in large perdeuterated proteins is proposed. It involves an alternative isotopic labeling protocol, the use of an out-and-back (13)C-(13)C TOCSY experiment ((H)C-TOCSY-C-TOCSY-(C)H) and an optimized non-uniform sampling protocol. It has
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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