5.08J | Spring 2016 | Undergraduate

Biological Chemistry II

Readings

Lecture reading assignments (by module) are listed below. For recitation reading assignments, please see the Recitation Readings and Handouts column in Lecture and Recitation Videos.

General Background (Lecture 1)

Required

Goodsell, D. S. “Inside a Living Cell.” Trends in Biochemical Sciences 16, no. 6 (1991): 203–6.

Minton, A. P. “How can Biochemical Reactions within Cells Differ from Those in Test Tubes?Journal of Cell Science 119 (2006): 2863–69.

Module 1: Translation (Lectures 2-7)

Required

Woorhees, R. M., and V. Ramakrishnan. “Structural Basis of the Translational Elongation Cycle.” Annual Review of Biochemistry 82 (2013): 203–36.

Optional

Zaher, H. S., and R. Green. “Fidelity at the Molecular Level: Lessons from Protein Synthesis.” Cell 136, no. 4 (2009): 746–62.

Kavaliauskas, D., P. Nissen, et al. “The Busiest of All Ribosomal Assistants: Elongation Factor Tu.” Biochemistry 51, no. 13 (2012): 2642–51.

Liu, C. C., and P. G. Shultz. “Adding New Chemistries to the Genetic Code.” Annual Review of Biochemistry 79 (2010): 413–44.

Module 2: Protein Folding (Lectures 8-11)

Required

Kim, Y. E., M. S. Hipp, et al. “Molecular Chaperone Functions in Protein Folding and Proteostasis.” Annual Review of Biochemistry 82 (2013): 323–55.

Optional

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.

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.

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.

Module 3: Protein Degradation (Lectures 12-14)

Required

Sauer, R. T., and T. A. Baker. “AAA+ Proteases: ATP-Fueled Machines of Protein Destruction.” Annual Review of Biochemistry 80 (2011): 587–612.

Optional

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]

———. “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]

Module 4: Polyketide and Nonribosomal Peptide Assembly Lines (Lectures 15-18)

Required

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.)

Module 5: Cholesterol Biosynthesis and Cholesterol Homeostasis (Lectures 19-25)

Required

Christianson, D. “Unearthing the Roots of the Terpenome.” Current Opinion in Chemical Biology 12, no. 2 (2008): 141–50.

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.

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.

Optional

Goldstein, Joseph L., R. A. DeBose-Boyd, et al. “Protein Sensors for Membrane Sterols.” Cell 124, no. 1 (2006): 35-46.

Goldstein, Joseph L., and Michael S. Brown. “History of Discovery: The LDL Receptor.” Arteriosclerosis, Thrombosis, and Vascular Biology 29, no. 4 (2009): 431–38.

Module 6: Metal Ion Homeostasis (Lectures 25-31)

Required

Frey, P. A., and G. H. Reed. “The Ubiquity of Iron.” ACS Chemical Biology 7, no. 9 (2012): 1477–81.

Optional

Wang, J., and K. Pantopoulos. “Regulation of Cellular Iron Metabolism.” Biochemical Journal 434, no. 3 (2010): 365–81.

Hammer, N. D., and E. P. Skaar. “Molecular Mechanisms of Staphylococcus Aureus Iron Acquisition.” Annual Review of Microbiology 65 (2011): 129–47.

Module 7: Reactive Oxygen Species (ROS) (Lectures 32-34)

Required

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.

Optional

Paulsen, C. E. “Peroxide-dependent Sulfenylation of the EFGR Catalytic Site Enhances Kinase Activity.” Nature Chemical Biology 8 (2011): 57–64.

Module 8: Nucleotide Metabolism (Lectures 34-36)

Required

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.)

Optional

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.

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.

Course Info

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Spring 2016
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