BIOL 200 Lecture Notes - Lecture 19: Protein Structure, Gtpase, Centrifugation

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17 Nov 2016
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Primary sequence doesn"t always tell us structure & function. Crystallography and x-ray diffraction can identify protein structure: protein crystals bombarded w/ x-rays (high energy beams, scatter pattern captured, used to generate electron density maps, analogy: throwing a rock into water; ripple pattern. Electron density maps: tell us about how proteins form/come tgthr; structure. Ligand: anything that could bind to a protein: can change protein function (via changing its conformation) Important e. g. : allosteric switches: tells us strength of a protein via kd. Smaller kd = higher affinity b/w the two proteins. Proteins as enzymes: lower ea, substrates" ability to come together, active sites: specific for a substrate. Where substrate binds: enzyme never gets consumed in a rxn, formation of enzyme-substrate complex -> formation of product -> liberation of products -> enzyme goes on to help other substrates. Vmax is the max. speed/rate of rxn where you reach a plateau; all your enzymes are in use, i. e. all active sites occupied.

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