BIOS 41 Chapter Notes - Chapter 4: Thrombin, Arginine, System For Information On Grey Literature In Europe
27 Feb 2017
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Document Summary
Proteins have many functions: enzymes, signaling, receptors, structural, transport, storage. Hydrogen bonds, electrostatic, van der walls, hydrophobic interactions. Conforms in a way that its free energy is minimized: the folding process is thus energetically favorable, as it releases heat and increases the disorder of the universe. Long polypeptide chains are very flexible-many of the peptide bonds that link the carbon atoms in the polypeptide backbone allow free rotation of the atoms they join. In aqueous solutions, hydrophobic molecules forced together to minimize their disruptive effect on the hydrogen-bonded network of the surrounding water molecules. Distribution of its polar and nonpolar amino acids: the nonpolar (hydrophobic) side chains -cluster in the interior of the folded protein. Can avoid the aqueous cytosol: polar side chains - arrange themselves near the outside of the folded protein. Can form hydrogen bonds with water and with other polar molecules.
