Biology 1002B Lecture Notes - Lecture 3: Macromolecular Crowding, Protein Folding, Hydrogen Bond
26 May 2016
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Cycle 1: trapping light for energy and information. For a protein to be functional, it needs to fold correctly. Primary sequence, as it comes off the ribosome, is just a polypeptide that has yet to fold, so it has no function. It is simply a sequence of amino acids. It needs to fold into its native conformation for it to be functional (tertiary) Folding occurs very fast in a cell (milliseconds) Conformation (shape) is simply a protein"s tertiary structure. The primary sequence itself has all the info required for the protein to get to the tertiary structure. Macromolecular crowding: in vitro: (test tube) 0. 1 mg/ml, in vivo: (a living cell) >300 mg/ml, macromolecular crowding can interfere with protein folding. Unfolded protein goes in, tertiary protein goes out. Do not affect in component of tertiary product (doesn"t dictate how it folds, just helps it fold) Human genome codes for hundreds of different chaperones. Different chaperones can fold different kinds of protein.
