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.
Because of their easy availability and their relative chemical stability, urea, formic acid, and glycine might have played a role in the assembly process of nucleobases. In this paper, a short reaction path is described to prepare hypoxanthine starting from
Langmuir : the ACS journal of surfaces and colloids, 23(10), 5406-5411 (2007-04-14)
Conformational behaviors of urea and glycinamide have been investigated using the B3LYP functional with the 6-311+G* and 6-311+G** basis sets. Urea monomers have nonplanar minima at all the levels studied, even in the aqueous phase. In the case of glycinamide
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
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
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