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Isobutanol (IUPAC nomenclature: 2-methylpropan-1-ol) is an organic compound with the formula (CH 3) 2 CHCH 2 OH (sometimes represented as i-BuOH). This colorless, flammable liquid with a characteristic smell is mainly used as a solvent either directly or as its esters.
Butanol (also called butyl alcohol) is a four-carbon alcohol with a formula of C 4 H 9 O H, which occurs in five isomeric structures (four structural isomers), from a straight-chain primary alcohol to a branched-chain tertiary alcohol; [1] all are a butyl or isobutyl group linked to a hydroxyl group (sometimes represented as BuOH, sec-BuOH, i-BuOH, and t-BuOH).
Structure of a typical L-alpha-amino acid in the "neutral" form. Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. [1] Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. [2] Only these 22 appear in the genetic code of life ...
Protein primary structure is the linear sequence of amino acids in a peptide or protein. [1] By convention, the primary structure of a protein is reported starting from the amino -terminal (N) end to the carboxyl -terminal (C) end.
1-Butanol, also known as butan-1-ol or n-butanol, is a primary alcohol with the chemical formula C 4 H 9 OH and a linear structure. Isomers of 1-butanol are isobutanol, butan-2-ol and tert-butanol. The unmodified term butanol usually refers to the straight chain isomer.
Like other butanols, butan-2-ol has low acute toxicity. The LD 50 is 4400 mg/kg (rat, oral). [6]Several explosions have been reported [7] [8] [9] during the conventional distillation of 2-butanol, apparently due to the buildup of peroxides with the boiling point higher than that of pure alcohol (and therefore concentrating in the still pot during distillation).
The primary structure (string of amino acids) of a protein ultimately encodes its uniquely folded three-dimensional (3D) conformation. [20] The most important factor governing the folding of a protein into 3D structure is the distribution of polar and non-polar side chains. [21]
The first widely used techniques to predict protein secondary structure from the amino acid sequence were the Chou–Fasman method [17] [18] [19] and the GOR method. [20] Although such methods claimed to achieve ~60% accurate in predicting which of the three states (helix/sheet/coil) a residue adopts, blind computing assessments later showed ...