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637858

Sigma-Aldrich

2-Keto-3-(methyl-d3)-butyric acid-1,2,3,4-13C4, 3-d sodium salt

99 atom % 13C, 98 atom % D, ≥99% (CP)

Sinónimos:

Sodium α-ketoisovalerate-3-(methyl-d3),1,2,3,4-13C4,3-d1

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About This Item

Fórmula lineal:
13CH313CD(CD3)13CO13CO2Na
Peso molecular:
146.09
MDL number:
MFCD06411303
UNSPSC Code:
12352106
PubChem Substance ID:
24882891
NACRES:
NA.12

isotopic purity

99 atom % 13C
98 atom % D

assay

≥99% (CP)

form

solid

technique(s)

bio NMR: suitable

mp

227-230 °C (lit.)

mass shift

M+8

SMILES string

[Na+].[2H]C([2H])([2H])[13C]([2H])([13CH3])[13C](=O)[13C]([O-])=O

InChI

1S/C5H8O3.Na/c1-3(2)4(6)5(7)8;/h3H,1-2H3,(H,7,8);/q;+1/p-1/i1D3,2+1,3+1D,4+1,5+1;

InChI key

WIQBZDCJCRFGKA-XCPSOYJTSA-M

Packaging

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.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificados de análisis (COA)

Lot/Batch Number
MBBB8926V
MBBB8784V
MBBB4642V
EB0273
TA1508V

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β-glucosidases have received considerable attention due to their essential role in bioethanol production from lignocellulosic biomass. β-glucosidase can hydrolyse cellobiose in cellulose degradation and its low activity has been considered as one of the main limiting steps in the process.
Soumya P Behera et al.
Nature communications, 11(1), 5547-5547 (2020-11-05)
Methyl-NMR enables atomic-resolution studies of structure and dynamics of large proteins in solution. However, resonance assignment remains challenging. The problem is to combine existing structural informational with sparse distance restraints and search for the most compatible assignment among the permutations.

Artículos

Selective Protonation of Methyl Groups in Highly Deuterated Proteins

Sigma-Aldrich presents an article about the selective protonation of methyl groups in highly deuterated proteins. In which the structural NMR studies of small proteins, a maximum number of proton chemical shifts are usually assigned and NOEs connecting large numbers of sites are subsequently quantified in terms of distance restraints that are then used to obtain an ensemble of structures.

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