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N-(2-amino-2-oxoethyl)-4-nitrobenzamide is a chemical compound with the molecular formula C9H9N3O4. It is an organic compound that features a benzamide group, which is a derivative of benzoic acid, where the carboxyl group is replaced by an amide group. The compound has a nitro group attached to the para position of the benzene ring, which imparts specific chemical properties. The 2-amino-2-oxoethyl group is connected to the nitrogen atom of the amide, providing amine and ketone functionalities. N-(2-amino-2-oxoethyl)-4-nitrobenzamide is known for its potential applications in the synthesis of pharmaceuticals and other organic compounds, particularly those with biological activity. It is important to note that the handling and use of such chemicals should be done with caution, adhering to safety protocols due to their potential reactivity and the presence of functional groups that can be sensitive to certain conditions.

5410-49-1

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5410-49-1 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 5410-49-1 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 5,4,1 and 0 respectively; the second part has 2 digits, 4 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 5410-49:
(6*5)+(5*4)+(4*1)+(3*0)+(2*4)+(1*9)=71
71 % 10 = 1
So 5410-49-1 is a valid CAS Registry Number.

5410-49-1Relevant academic research and scientific papers

New charge-bearing amino acid residues that promote β-sheet secondary structure

Maynard, Stacy J.,Almeida, Aaron M.,Yoshimi, Yasuharu,Gellman, Samuel H.

supporting information, p. 16683 - 16688 (2015/02/05)

Proteinogenic amino acid residues that promote β-sheet secondary structure are hydrophobic (e.g., Ile or Val) or only moderately polar (e.g., Thr). The design of peptides intended to display β-sheet secondary structure in water typically requires one set of residues to ensure conformational stability and an orthogonal set, with charged side chains, to ensure aqueous solubility and discourage self-association. Here we describe new amino acids that manifest substantial β-sheet propensity, by virtue of β-branching, and also bear an ionizable group in the side chain.

Stabilizing and destabilizing effects of phenylalanine → F 5-phenylalanine mutations on the folding of a small protein

Woll, Matthew G.,Hadley, Erik B.,Mecozzi, Sandro,Gellman, Samuel H.

, p. 15932 - 15933 (2007/10/03)

We report a systematic evaluation of phenylalanine-to-pentafluorophenylalanine (Phe → F5-Phe) mutants for the 35-residue chicken villin headpiece subdomain (c-VHP), the hydrophobic core of which features a cluster of three Phe side chains (residues 6, 10, and 17). Phe → F5-Phe mutations are interesting because aryl-perfluoroaryl interactions of optimal geometry are intrinsically more favorable than aryl-aryl interactions and because perfluoroaryl units are more hydrophobic than are analogous aryl units. One mutant, Phe-10 → F5-Phe, provides enhanced tertiary structural stability relative to the native sequence. The other six mutants analyzed caused a decrease in stability. Copyright

Substituent effect on acidity of substituted 2-(4-nitrobenzoylamino)alkanamidesin methanol-dimethyl sulfoxide mixtures

Mitas, Petr,Sedlak, Milos,Kavalek, Jaromir

, p. 85 - 93 (2007/10/03)

The dissociation constants of substituted 2-(4-nitrobenzoylamino)alkanamides, N-[2-(4-nitrobenzoylamino)aikanoyl]pyrrolidines, and N-alkyl-4-nitrobenzamides have been measured spectrophotometrically in 60 and 80% v/v DMSO. The pKA values of these N-acids are discussed from the point of view of substituents at the acetamide a-carbon atom.

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