L'asparagine, classified as a non-essential amino acid, is an essential building block in the biosynthesis of proteins and is encoded in messenger RNA by the codons AAU and AAC. Its molecular structure involves the amidification of the carboxyl terminal of aspartate, resulting in the formation of electrically neutral polar residues that exhibit a tendency to form hydrogen bonds through its amide group. With a van der Waals radius measuring 96 Å, this amino acid plays a crucial role in the intricate processes of protein folding and molecular interactions within cellular systems.
Furthermore, the multifaceted nature of asparagine extends to its active participation in various metabolic pathways, including the biosynthesis of glycoproteins, which are integral components in cellular recognition and adhesion. Additionally, asparagine serves as a vital precursor for the synthesis of important signaling molecules and cellular messengers, contributing significantly to the modulation of cellular responses and the regulation of physiological functions.
The intricate interplay of asparagine in the complex network of cellular processes emphasizes its indispensable role in maintaining cellular homeostasis and supporting fundamental biological functions. Its multifunctional properties underscore the significance of asparagine in various biochemical and physiological pathways, highlighting its essential contribution to the intricate tapestry of cellular life.
Asparagine, denoted by the symbol Asn or N, represents an essential component in the intricate machinery of protein biosynthesis. Structurally, it encompasses an α-amino group, typically found in the protonated −NH+ 3 configuration under physiological conditions, alongside an α-carboxylic acid group, prevailing in the deprotonated −COO− form within the biological milieu. Its distinctive side chain carboxamide further classifies it as a polar, aliphatic amino acid, imparting essential characteristics crucial for its functional diversity and participation in cellular processes.
In the context of human physiology, asparagine is deemed non-essential, as the human body possesses the capacity to endogenously synthesize it. This pivotal amino acid finds its genetic instructions encoded by the specific codons AAU and AAC, underscoring its indispensable role in the intricate orchestration of protein assembly and cellular function. Its dynamic participation in the intricate framework of molecular interactions emphasizes its significance in the complex landscape of biological processes, reflecting its vital contribution to the multifaceted tapestry of life-sustaining mechanisms.
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Config Rule :
config('L-asparagine',[ substituent(aminoacid_L_backbone), substituent(methandiylamide), linkage(from(aminoacid_L_backbone,car(1)), to(methandiylamide,car(1)), down,single)]). %%%% Substituent Config Rules for compound 'L-asparagine' %%%% config(aminoacid_L_backbone,[ left(amino), right(hyd), top(carboxyl), center(car(1))]). config(methandiylamide,[ top(methandiyl(1,empty)), center(keto(2,amine))]).
Smiles String :
Fischer Diagram :
The Terminals for all the Config Rules are in Prolog Definite Clause Grammar (DCG) form.They can be checked in the Manual here.
The compound's PDB file can be seen here.