BIOL 1400 Lecture Notes - Lecture 4: Activation Energy, Protein Kinase, X-Ray Crystallography
Document Summary
A chain of proteins connected by covalent peptide bonds (polypeptides). A repeating sequence of atoms found in every amino acid (-n-c-c-). Many weak noncovalent bonds that form within the protein. Atoms in the polypeptide backbone and the amino acid side chains. Hydrogen bonds, electrostatic attractions, hydrophobic interactions, and van der waals attractions. The noncovalent bonds are weak compared to covalent bonds. The distribution of polar and nonpolar amino acids. Energetic considerations (lowest structure where the free energy is minimized). Treatment with solvents that disrupt the noncovalent interactions holding the folded chain together. A protein is folded back into its original conformation. The denaturing solvent is removed (must be under the right conditions). A misfolded protein that can convert the properly folded version into an abnormal conformation. Urea functions as both a hydrogen-bond donor (nh2 groups) and acceptor (c=o groups) which allows it to squeeze between hydrogen bonds and destabilize the protein.
