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Merck
CN

V900686

Sigma-Aldrich

N-Acetylglycine

Vetec™, reagent grade, 98%

Synonym(s):

Acetamidoacetic acid, Aceturic acid

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About This Item

Linear Formula:
CH3CONHCH2CO2H
CAS Number:
543-24-8
Molecular Weight:
117.10
Beilstein:
774114
EC Number:
208-839-6
MDL number:
MFCD00004275
UNSPSC Code:
12352209
PubChem Substance ID:
329830058

Key Documents

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grade

reagent grade

product line

Vetec™

Assay

98%

form

powder or crystals

reaction suitability

reaction type: solution phase peptide synthesis

color

white

mp

207-209 °C (lit.)

SMILES string

CC(=O)NCC(O)=O

InChI

1S/C4H7NO3/c1-3(6)5-2-4(7)8/h2H2,1H3,(H,5,6)(H,7,8)

InChI key

OKJIRPAQVSHGFK-UHFFFAOYSA-N

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Legal Information

Vetec is a trademark of Merck KGaA, Darmstadt, Germany

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
WXBC4859V
WXBB1187
STBB2380V

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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
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
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
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
Liangxing Wu et al.
Journal of the American Chemical Society, 130(12), 4089-4096 (2008-03-07)
Eight B-containing compounds, i.e., 1a-h, were prepared as mimics of the green fluorescent protein (GFP) fluorophore. The underlying concept was that synthetic GFP chromophore analogues are not fluorescent primarily because of free rotation about an aryl-alkene bond (Figure 1b). This
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