BIO 327 Chapter Notes - Chapter 4: Protein Folding, Lipid Bilayer, Amine
Document Summary
The main building blocks from which cells are assembled. The shape of a protein is determined by its amino acid sequence. C-terminus- the end with the free carboxyl group. Amino acid side chains are not involved in forming peptide bonds. Protein shape is determined by noncovalent bonds (hydrogen bonds, electrostatic attractions, van der waals attractions) and hydrophobic interactions. Nonpolar hydrophobic side chains tend to cluster in the interior of the folded protein. Proteins fold into a conformation of lowest energy. Protein folding is assisted by chaperone proteins, making the process more efficient. A single polypeptide chain turns around itself to form a rigid cylinder. Sheets: polypeptide chains lay side by side. Form rigid structures at the core of many proteins. Parallel sheets run in the same orientation. Secondary structure- form within certain sequences in the polypeptide chain, include helix and sheets. Tertiary structure- the full 3d conformation formed by an entire polypeptide chain.
