MCB 181L Lecture Notes - Lecture 6: Cysteine, Protein Folding, Electronegativity

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Properties: size/length rings are larger (take up more space, flexibility long & linear=more flexibility, charge based on electronegativity. Proline: helps make turns and kinks in proteins. Protein is simply a long chain of amino acids. Covalent bonds between adjacent amino acids are called peptide bonds. Amino acids are connected between the amino acid carboxyl groups. Secondary structure: a helices and b sheets joined by hydrogen bonds. Tertiary structure: geometric shape, interaction of secondary structures, determined by interaction of r-groups. H bonds, hydrophobic interactions, electrostatic interactions, disulfide bonds. Oil/water not mixing, protein folding, membrane formation all same principle. Hydrophobic residues (amino acids) are found on the inside but, if a (+) amino acid had a (-) amino acid to interact with on the inside, they would both be happy . Oxygen binds to heme group on hemoglobin: 2 oxygen atoms (non-polar) share equally.

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