MCB 244 Lecture Notes - Lecture 1: Alpha Helix, Beta Sheet, Complete Protein

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Lipids- for energy storage, cellular components, synthesis of bioactive compounds. Carboxyl tail of amino acid, removal of water result in peptide bond. E groups- place where amino acids show wide combos. Nonpolar, polar, charged, special fcns amino acids. Made of linear sequence of amino acids bonded together thru covalent peptide bonds. Give some degree of flexibility to many globular proteins. Final 3d shape exhibited by one complete protein chain. Fold into compact, nearly spherical shape such as enzymes. Only present in proteins with 2 or more protein strands. Prosthetic group- non protein structure covalently bonded to the protein. Rate of chemical rxn may be increased with enzyme concentration or increase in substrate concentration. But increase in rate substrate conc. increases the rate of rxn only up to point of saturation of the enzyme. Competitive inhibitors-resembles substrate and binds to active site of enzyme, compete with each other for occupation of the active site.

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