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线性分子式:
NH2CH2CONH2 · HCl
化学文摘社编号:
分子量:
110.54
UNSPSC Code:
12352100
NACRES:
NA.22
PubChem Substance ID:
EC Number:
216-789-1
Beilstein/REAXYS Number:
3554199
MDL number:
Assay:
98%
InChI
1S/C2H6N2O.ClH/c3-1-2(4)5;/h1,3H2,(H2,4,5);1H
InChI key
WKNMKGVLOWGGOU-UHFFFAOYSA-N
SMILES string
Cl.NCC(N)=O
assay
98%
mp
204 °C (dec.) (lit.)
Quality Level
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Application
在生理 pH 值范围内可用的缓冲剂。
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Gottfried K Schroeder et al.
Biochemistry, 46(13), 4037-4044 (2007-03-14)
As a model for mechanistic comparison with peptidyl transfer within the ribosome, the reaction of aqueous glycinamide with N-formylphenylalanine trifluoroethyl ester (fPhe-TFE) represents an improvement over earlier model reactions involving Tris. The acidity of trifluoroethanol (pKa 12.4) resembles that of
Irene M Lagoja et al.
Chemistry & biodiversity, 2(7), 923-927 (2006-12-29)
A possible reaction mechanism for the dehydration of glycinamide (3) and N,N'-diformylurea (4) yielding hypoxanthine (2) has been investigated. Furthermore, a potential prebiotic route converting hypoxanthine (2) into adenine (1) via phosphate activation followed by substitution reaction with NH3 was
Len Ito et al.
FEBS letters, 585(3), 555-560 (2011-01-18)
Glycine amide (GlyAd), a typically amidated amino acid, is a versatile additive that suppresses protein aggregation during refolding, heat treatment, and crystallization. In spite of its effectiveness, the exact mechanism by which GlyAd suppresses protein aggregation remains to be elucidated.
Samir Abdurahman et al.
Antimicrobial agents and chemotherapy, 52(10), 3737-3744 (2008-07-23)
Upon maturation of the human immunodeficiency virus type 1 (HIV-1) virion, proteolytic cleavage of the Gag precursor protein by the viral protease is followed by morphological changes of the capsid protein p24, which will ultimately transform the virus core from
Stefan Glatzel et al.
Chemical communications (Cambridge, England), 46(25), 4517-4519 (2010-05-21)
Homopolymers of N-acryloyl glycinamide were prepared by reversible addition-fragmentation chain transfer polymerization in water. The formed macromolecules exhibit strong polymer-polymer interactions in aqueous milieu and therefore form thermoreversible physical hydrogels in pure water, physiological buffer or cell medium.
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