BIOLOGY 2B03 Chapter Notes - Chapter 1: Intron, Histidine, Phenylalanine
7 Apr 2018
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Document Summary
Review principles of primary structure of a polypeptide. Overview of properties of amino acid variable r-groups. Describe chemical interactions essential to protein structure. Sensors for environmental changes and mechanisms for relaying this information to the cell. There are 20 different amino acids that create proteins. Post-translational modifications can alter properties of individual amino acids and whole protein. Amino acid: contains an alpha carbon, an amino group, a carboxyl group and a r group. They are classified into groups based on solubility in water or polarity of the side chain: side chains differ in size, shape, charge, hydrophobicity, reactivity. Solubility: refers to physical property of molecule that can transiently bond with water. Hydrophobic molecule: not electrically polarized, repels water. Hydrophobic molecules are usually found in interior of cytosolic proteins and form a hydrophobic core. Protein found in a hydrophobic environment such as membrane will have opposite structure with hydrophobic amino acids accumulating on the exterior of the protein.
