BCH 6743 Biochemical Energetics
(Section 1715)
Time: One hour per week, 3:00-4:00 p.m. (8th period)
Room ARB 3-265
Course Coordinator: Dr. Chun, Room: MSB 355
(http://www.med.ufl.edu/biochem/BCH6743/syl2002.doc)
Course Syllabus
Rated courses for IDP students
This 15 lecture-discussion module will focus on the molecular and structural interpretation of energy transformation in biological systems, including the mechanism of F1F2-type ATP synthase, a biological rotary motor; a proton motive force operating across many energy-conserving biological membrane; molecular chaperones in cytosol, from nascent chain to folded protein; the energy landscape of protein folding, and the role of the thermodynamic molecular switch in biological systems. In the context of these macromolecular interactions, methods of simple thermodynamic analysis will be introduced.
Course Syllabus
1. The F1F2-type ATP synthase is a key enzyme in cellular energy inter- conversion during ATP synthesis, this large protein complex uses a proton gradient and associated membrane potential to synthesize ATP. It can also reverse and hydrolyze ATP to generate a proton gradient. Although both motors can work separately, they must be connected together to inter-convert energy (2 lecture-discussions).
2. A proton motive force (PMF) has been detected across many energy-conserving biological membranes, with proton translocation being driven by membrane-associated protein that could provide electron flow from low-redox potential electron donors to high potential electron acceptors (2 lecture-discussions).
3. Molecular chaperones in cytosol, from nascent chain to folded protein. This unit examines recent advances in our mechanistic understanding of de novo protein folding in cytosol and seeks to provide a coherent view of the overall flux of newly synthesized protein through the chaperone system (2 lecture-discussions)
4. Water in molecular orientation. This unit examines how water provides the impetus for molecular recognition in aqueous solution. Crystallization must involve molecular recognition. As the solvent content is reduced, the collision between molecules increases until it becomes energetically more favorable for them to nucleate rather than solvate. Therefore the molecules deposit on the crystal surface in the correct orientation (1 lecture and discussions).
5. The critical factor driving the sequence-specific hydrophobic interaction is a temperature-dependent heat capacity change of reaction, which is positive at low temperature but switches to a negative value at a temperature well below the ambient range. This determines the thermodynamic behavior patterns of the Gibbs free energy change, and hence a change in the equilibrium constant, Keq and/or spontaneity of reaction. This thermodynamic molecular switch is a universal feature of biological systems (4 lecture-discussions).
6. The innate thermodynamic quantities in protein unfolding. The difference in
the innate temperature-invariant enthalpy between folded and unfolded forms is generally small, as little as 2-17 kcal mol-1, whereas the thermal agitation energy is approximately 10 times greater than that of the innate temperature-invariant enthalpy (3 lecture-discussions)
Grading criteria: This module consists of 14 lectures, each followed by 20
minutes of discussion. One lecture is reserved for student presentations. Each topic will have references and reading materials which will be handed out prior to the lecture series. Student input in these discussions is expected. Grading will be based on 30 minute presentations of topics assigned. A letter grade will be given.
Prerequisite: BCH 3025, CHM 3218, CHM 4207, or consent of instructor; see course description under Medical Science-Biochemistry and molecular biology.
Reading material: Students should have access to:
Pertinent journal articles
Advances in Protein Chemistry
Methods in Enzymology
Reviews in Science, Biochemistry, and Journal of Biological Chemistry
Lecture notes will be available