MICR 803 Lecture Notes - Lecture 1: Disulfide, Alpha Helix, Protein Folding

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Primary: sequence of amino acids in the polypeptide chain. Sequence determined by the dna that encodes for that protein. Changing one amino acid can change the proteins sequence, can affect proteins overall structure and function. Secondary structure: local folded structures that form within a polypeptide due to interaction between atoms of the back bone. Secondary structure does not involve the r groups (key) Alpha helix and b sheets are held in shape by h bonds which form between the carbonyl o of one acid and the amino h of another (carbonyl and amino groups) Proline and glycine not compatible with helix formation. Tertiary structure: due to interactions between the r groups of amino acids that make up the protein (hydrogen bonding, ion bonding etc) all cov bonds. Hydrophobic interactions: the amino acids are non polar, hydrophobic r groups cluster together inside the proteins, leaving hydrophilic amino acids on the outside to interact with water molecules, cytosal.

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