Fundamentals of Chemical Biology

Readings

• Goodsell, D. S. “ Inside a Living Cell .” Trends in Biochemical Sciences 16, no. 6 (1991): 203–6. ↗
  Required
• Minton, A. P. “ How can Biochemical Reactions within Cells Differ from Those in Test Tubes? ” Journal of Cell Science 119 (2006): 2863–69. ↗
  Required
• Woorhees, R. M., and V. Ramakrishnan. “ Structural Basis of the Translational Elongation Cycle .” Annual Review of Biochemistry 82 (2013): 203–36. ↗
  Required
• Zaher, H. S., and R. Green. “ Fidelity at the Molecular Level: Lessons from Protein Synthesis .” Cell 136, no. 4 (2009): 746–62. ↗
  Recommended
• Kavaliauskas, D., P. Nissen, et al. “ The Busiest of All Ribosomal Assistants: Elongation Factor Tu .” Biochemistry 51, no. 13 (2012): 2642–51. ↗
  Recommended
• Liu, C. C., and P. G. Shultz. “ Adding New Chemistries to the Genetic Code .” Annual Review of Biochemistry 79 (2010): 413–44. ↗
  Recommended
• Kim, Y. E., M. S. Hipp, et al. “ Molecular Chaperone Functions in Protein Folding and Proteostasis .” Annual Review of Biochemistry 82 (2013): 323–55. ↗
  Required
• Hartl, F. U., and M. Hayer-Hartl. “ Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein .” Science 295, no. 5561 (2002): 1852–58. ↗
  Recommended
• Young, J. C., V. R. Agashe, et al. “ Pathways of Chaperone-Medicated Protein Folding in the Cytosol .” Nature Reviews Molecular Cell Biology 5 (2004): 781–91. ↗
  Recommended
• Nakamoto, H., and J. C. A. Bardwell. “ Catalysis of Disulfide Bond Formation and Isomerization in the Escherichia Coli Periplasm .” Biochimica et Biophysica Acta (BBA) 1694, no. 1–3 (2004): 111–19. ↗
  Recommended
• Sauer, R. T., and T. A. Baker. “ AAA+ Proteases: ATP-Fueled Machines of Protein Destruction .” Annual Review of Biochemistry 80 (2011): 587–612. ↗
  Required
• Walsh, C. T. “Proteolytic Posttranslational Modification of Proteins.” Chapter 8 in Posttranslational Modification of Proteins: Expanding Nature’s Inventory . W. H. Freeman, 2005. ISBN: 9780974707730. [Preview with Google Books ] ↗
  Recommended
• ———. “Ubiquitin and Ubiquitin-Like Protein Tags.” Chapter 9 in Posttranslational Modification of Proteins: Expanding Nature’s Inventory . W. H. Freeman, 2005. ISBN: 9780974707730. [Preview with Google Books ] ↗
  Recommended
• Fischbach, M. A., and C. T. Walsh. “ Assembly-Line Enzymology for Polyketide and Nonribosomal Peptide Antibiotics: Logic, Machinery, and Mechanisms .” Chemical Reviews 106, no. 8 (2006): 3468–96. (Read sections 1–3. Later sections are optional.) ↗
  Required
• Christianson, D. “ Unearthing the Roots of the Terpenome .” Current Opinion in Chemical Biology 12, no. 2 (2008): 141–50. ↗
  Required
• Goldstein, Joseph L., and Michael S. Brown. “ A Century of Cholesterol and Coronaries: From Plaques to Genes and Statins .” Cell 161, no. 1 (2015): 161–72. ↗
  Required
• Voet, Voet, and Pratt. “Lipid Metabolism.” Chapter 20 in Fundamentals of Biochemistry: Life at the Molecular Level . 4th ed. Wiley, 2015, pp. 657–64, 678–81, and 700–709. ISBN: 9780470547847.
  Required
• Goldstein, Joseph L., R. A. DeBose-Boyd, et al. “ Protein Sensors for Membrane Sterols .” Cell 124, no. 1 (2006): 35-46. ↗
  Recommended
• Goldstein, Joseph L., and Michael S. Brown. “ History of Discovery: The LDL Receptor .” Arteriosclerosis, Thrombosis, and Vascular Biology 29, no. 4 (2009): 431–38. ↗
  Recommended
• Frey, P. A., and G. H. Reed. “ The Ubiquity of Iron .” ACS Chemical Biology 7, no. 9 (2012): 1477–81. ↗
  Required
• Wang, J., and K. Pantopoulos. “ Regulation of Cellular Iron Metabolism .” Biochemical Journal 434, no. 3 (2010): 365–81. ↗
  Recommended
• Hammer, N. D., and E. P. Skaar. “ Molecular Mechanisms of Staphylococcus Aureus Iron Acquisition .” Annual Review of Microbiology 65 (2011): 129–47. ↗
  Recommended
• Winterbourn, C. C., and A. J. Kettle. “ Redox Reactions and Microbial Killing in the Neutrophil Phagosome .” Antioxidants and Redox Signaling 18, no. 6 (2013): 642–60. ↗
  Required
• Paulsen, C. E. “ Peroxide-dependent Sulfenylation of the EFGR Catalytic Site Enhances Kinase Activity .” Nature Chemical Biology 8 (2011): 57–64. ↗
  Recommended
• Voet, Voet, and Pratt. Chapters 5, 28, and 29 in Fundamentals of Biochemistry: Life at the Molecular Level . 4th ed. Wiley, 2015. ISBN: 9780470547847. (Introductory Biochemistry textbook that covers purine and pyrimidine biosynthesis and deoxynucleotide biosynthesis.)
  Required
• Zhao, H., J. B. French, et al. “ The Purinosome, a Multi-protein Complex Involved in the De Novo Biosynthesis of Purines in Humans .” Chemical Communications 49 (2013): 4444–52. ↗
  Recommended
• E. Minnihan, D. G. Nocera, et al. “ Reversible, Long-Range Radical Transfer in E. coli Class la Ribonucleotide Reductase .” Accounts of Chemical Research 46, no. 11 (2013): 2524–35. ↗
  Recommended
• There is no required textbook for this course. However, a general biochemistry book is strongly recommended for background material, such as:
  Required
• Voet, D., J. Voet, and C. Pratt. Fundamentals of Biochemistry: Life at the Molecular Level . 4th ed. Wiley, 2015. ISBN: 9780470547847.
  Required