BIO 327 Lecture Notes - Lecture 4: Open Reading Frame, Start Codon, Peptide
Document Summary
Enzymes, structural proteins, transport, motor, storage, signaling receptors, gene regulators, or other special purposes. There are basic rules that govern their structures. Proteins fold into conformations that represent energy minima. Nonpolar side chains like to bury within themselves to avoid the water. Molecular chaperones in the cell help proteins fold into the correct conformation. Not all possible protein sequences are used by nature. Few of the sequences create structures with stable energy minima. Need a structure with start codon, open reading frame, stop codon. Tertiary- 3d organization of secondary structures, protein domains. Relevant parts of the protein are polypeptide backbone and the side chains/r groups of each specific amino acid. Conditions that disrupt noncovalent bonds- heat energy, change in charges/ ions, cause the proteins to denature. Proteins can often refold by themselves in solution. Can occur between r groups/ parts of polypeptide backbone. Includes h-bonds, van der waals attractions, electrostatic attractions.
