Proteins (Unit 1) Flashcards
Proteins
Polymer of many amino acids folded into a 3D structure that specifies its region
Protein Functions
Catalyze chemical reactions, provide structural support, Transport substances, Regulate cell processes, Provide defence from disease
Amino Acids
Building blocks of proteins
Components of amino acids
Amino group and carboxyl group
Types of amino acids
20 different acids - 12 natural, 8 essential. Can be polar (R contains N,O,S), nonpolar (R contains only C) or carry a charge
Structure of Proteins
Primary, Secondary, Tertiary, Quaternary
Primary Structure
Peptide Chain. AA are joined by peptide linkages through condensation. Hydroxyl of carboxyl and hydrogen from amino is lost.
Secondary Structure
H Bonds between carbonyl of one bond and amino of other. Can form alpha helix (spiral) or beta pleated sheet (layers)
Tertiary Structure
Protein folding is due to/stabilized by intermolecular interactions between side chains of amino acids. Disulphide bonds can form with two sulfhydryl groups. H-bonds, Hydrophilic, and Hydrophobic, all influence group location during folding. Salt bridge
Salt Bridge
Electrostatic attractions between electrically charged amino acid side chains
Quaternary Structures
Occurs if more than 2 polypeptides make up protein. Join through intermolecular, and sometimes covalent interactions
Denaturation
Intermolecular forces in proteins are broken, so will lose shape and stop performing functions
Causes of Denaturation
Temperature, pH, chemicals