CHEM 153A Study Guide - Final Guide: Protein Structure, Ribonucleotide, Ribbon Diagram
15 Jun 2016
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_ribbon diagram (just the backbone atoms, emphasize secondary structure) No space within protein structures = allow weak interactions to form and stabilize the native configuration (tertiary structure) Oligomeric proteins (organic molecules must have quaternary structures) Metal ions b. coenzymes (organic cofactor: cosubstrates (transiently associated with ligands, prosthetic groups (permanently associated with ligands) Span on membranes interact with highly hydrophobic environment different polar/non-polar surface. Primary: accurate sequence of amino acids, determine structure. Experiment: isolate ribonucleotide with urea denature using base to reduce s-s bonds unfold protein (i. e. non- functional) remove urea to recreate s-s bonds gain original functions unfolding => denaturation => refolding renaturation. *** % decrease in folding = % unfolding: essential for understanding protein function. _id mutations that result in diseases (cid:0) diagnosis and effective therapies. Mutations don"t always affect structure: sequence determination. Account for untranslated regions (introns, utr, enzymatically removed chains from the final protein structure) Can also detect posttranslational modifications (target the regulations of proteins)
