V900686
N-Acetylglycine
Vetec™, reagent grade, 98%
Synonym(s):
Acetamidoacetic acid, Aceturic acid
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About This Item
Linear Formula:
CH3CONHCH2CO2H
CAS Number:
Molecular Weight:
117.10
EC Number:
208-839-6
UNSPSC Code:
12352209
PubChem Substance ID:
Beilstein/REAXYS Number:
774114
MDL number:
InChI key
OKJIRPAQVSHGFK-UHFFFAOYSA-N
InChI
1S/C4H7NO3/c1-3(6)5-2-4(7)8/h2H2,1H3,(H,5,6)(H,7,8)
SMILES string
CC(=O)NCC(O)=O
grade
reagent grade
product line
Vetec™
assay
98%
form
powder or crystals
reaction suitability
reaction type: solution phase peptide synthesis
color
white
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Legal Information
Vetec is a trademark of Merck KGaA, Darmstadt, Germany
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Anatoliy Volkov et al.
Journal of computational chemistry, 25(7), 921-934 (2004-03-18)
Accurate and fast evaluation of electrostatic interactions in molecular systems is still one of the most challenging tasks in the rapidly advancing field of macromolecular chemistry, including molecular recognition, protein modeling and drug design. One of the most convenient and
Z Gu et al.
Journal of magnetic resonance (San Diego, Calif. : 1997), 138(2), 193-198 (1999-05-26)
Triple-resonance experiments capable of correlating directly bonded and proximate carbon and nitrogen backbone sites of uniformly 13C- and 15N-labeled peptides in stationary oriented samples are described. The pulse sequences integrate cross-polarization from 1H to 13C and from 13C to 15N
S Zhang et al.
Journal of magnetic resonance (San Diego, Calif. : 1997), 132(1), 81-87 (1998-06-06)
A Gaussian-shaped, offset-independent adiabatic decoupling is adopted to decouple 13CO from 13C alpha or vice versa for 13C- and 15N-double-labeled proteins, together with a compensating decoupling applied on the opposite side of the 13C alpha resonance frequency. In a quite
Y Chen et al.
Biochemistry, 37(28), 9976-9982 (1998-07-17)
A general approach to dissecting the complex photophysics of tryptophan is presented and used to elucidate the effects of amino acid functional groups on tryptophan fluorescence. We have definitively identified the amino acid side chains that quench tryptophan fluorescence and
S K Mehta et al.
Journal of colloid and interface science, 314(2), 689-698 (2007-06-26)
The well-characterized, monodisperse nature of reverse micelles formed by sodium bis-(2-ethylhexyl)sulfosuccinate/water/isooctane and their usefulness in assimilating compounds of varied interests have been exploited to investigate the effect of acetyl modified amino acids (MAA) viz., N-acetyl-L-glycine (NAG), N-acetyl-L-aspartic acid (NAA) and
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