Arginine is the amino acid with the formula CN(CH₂)₃CHCO₂H. The molecule features a guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated and both the amino and guanidino groups are protonated, resulting in a cation.
Arginine is the amino acid with the formula (H2N)(HN)CN(H)(CH2)3CH(NH2)CO2H. The molecule features a guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO2−) and both the amino and guanidino groups are protonated, resulting in a cation. Only the l-arginine (symbol Arg or R) enantiomer is found naturally.[1] Arg residues are common components of proteins. It is encoded by the codons CGU, CGC, CGA, CGG, AGA, and AGG. [2] The guanidine group in arginine is the precursor for the biosynthesis of nitric oxide.[3] Like all amino acids, it is a white, water-soluble solid.
Explanation:
Arginine was first isolated in 1886 from yellow lupin seedlings by the German chemist Ernst Schulze and his assistant Ernst Steiger.[4][5] He named it from the Greek árgyros (ἄργυρος) meaning "silver" due to the silver-white appearance of arginine nitrate crystals.[6] In 1897, Schulze and Ernst Winterstein (1865–1949) determined the structure of arginine.[7] Schulze and Winterstein synthesized arginine from ornithine and cyanamide in 1899,[8] but some doubts about arginine's structure lingered[9] until Sørensen's synthesis of 1910.[10]
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Answer:
Arginine is the amino acid with the formula CN(CH₂)₃CHCO₂H. The molecule features a guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated and both the amino and guanidino groups are protonated, resulting in a cation.
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Answer:
Arginine is the amino acid with the formula (H2N)(HN)CN(H)(CH2)3CH(NH2)CO2H. The molecule features a guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO2−) and both the amino and guanidino groups are protonated, resulting in a cation. Only the l-arginine (symbol Arg or R) enantiomer is found naturally.[1] Arg residues are common components of proteins. It is encoded by the codons CGU, CGC, CGA, CGG, AGA, and AGG. [2] The guanidine group in arginine is the precursor for the biosynthesis of nitric oxide.[3] Like all amino acids, it is a white, water-soluble solid.
Explanation:
Arginine was first isolated in 1886 from yellow lupin seedlings by the German chemist Ernst Schulze and his assistant Ernst Steiger.[4][5] He named it from the Greek árgyros (ἄργυρος) meaning "silver" due to the silver-white appearance of arginine nitrate crystals.[6] In 1897, Schulze and Ernst Winterstein (1865–1949) determined the structure of arginine.[7] Schulze and Winterstein synthesized arginine from ornithine and cyanamide in 1899,[8] but some doubts about arginine's structure lingered[9] until Sørensen's synthesis of 1910.[10]
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