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The Fiesselmann thiophene synthesis is a name reaction in organic chemistry that allows for the generation of 3-hydroxy-2-thiophenecarboxylic acid derivatives from α,β-acetylenic esters with thioglycolic acid and its derivatives under the presence of a base. The reaction was developed by Hans Fiesselmann in the 1950s.
Glucose can exist in both a straight-chain and ring form. Two specific further subcategories of tautomerizations: Annular tautomerism is a type of prototropic tautomerism wherein a proton can occupy two or more positions of the heterocyclic systems found in many drugs, for example, 1 H - and 3 H - imidazole ; 1 H -, 2 H - and 4 H - 1,2,4 ...
Amino acid biosynthesis is the set of biochemical processes (metabolic pathways) by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids ...
These chains are linear and unbranched, with each amino acid residue within the chain attached to two neighboring amino acids. In nature, the process of making proteins encoded by RNA genetic material is called translation and involves the step-by-step addition of amino acids to a growing protein chain by a ribozyme that is called a ribosome. [58]
Contributing structures of the carbonate ion. In chemistry, resonance, also called mesomerism, is a way of describing bonding in certain molecules or polyatomic ions by the combination of several contributing structures (or forms, [1] also variously known as resonance structures or canonical structures) into a resonance hybrid (or hybrid structure) in valence bond theory.
Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a
The pH-dependence of the activity displayed by enzymes and the pH-dependence of protein stability, for example, are properties that are determined by the pK a values of amino acid side chains. The pK a values of an amino acid side chain in solution is typically inferred from the pK a values of model compounds (compounds that are similar to the ...
The side chains of the standard amino acids have a variety of chemical structures and properties, and it is the combined effect of all amino acids that determines its three-dimensional structure and chemical reactivity. [35] The amino acids in a polypeptide chain are linked by peptide bonds between amino and carboxyl