Textbook Reading: Voet & Voet, Biochemistry, 3rd Edition, Chapter 12, sections 1-3. (Membrane assembly, protein targeting, and plasma lipoproteins will not be covered here.)
Some recent articles
J. A. Killian & G. von Heijne (2000) "How proteins adapt to a membrane-water interface," Trends in Biochem. Sci. 25: 429-434.
R. M. Garavito & S. Ferguson-Miller (2001) "Detergents as tools in membrane biochemistry," J. Biol. Chem. 276: 32403-32406.
M. Edidin (2003) "The state of lipid rafts: from model membranes to cells," Annu. Rev. Biophys. Biomol. Struct. 32: 257-283.
M.-J. Bijlmakers & M. Marsh (2003) "The on-off story of protein palmitoylation," Trends in Cell Biol. 13: 32-42.
H. M. McConnell & M. Vrljic (2003) "Liquid-liquid immiscibility in membranes," Annu. Rev. Biophys. Biomol. Struct. 32: 469-492.
P. F. Devaux & R. Morris (2004) "Transmembrane asymmetry and lateral domains in biological membranes," Traffic 5: 241-246.
S. Degroote, J. Wolthoorn & G. van Meer (2004) "The cell biology of glycosphingolipids," Seminars in Cell & Develop. Biol. 15: 375-387.
S. Mukherjee & F. R. Maxfield (2004) "Membrane domains," Annu. Rev. Cell Dev. Biol. 20: 839-866.
T. Balla (2005) "Inositol-lipid binding motifs: signal integrators through protein-lipid and protein-protein interactions," J. Cell Sci. 118: 2093-2104.
L. Rajendran & K. Simons (2005) "Lipid rafts and membrane dynamics," J. Cell Sci. 118: 1099-1102.
A. Kusumi, C. Nakada, K. Ritchie, K. Murase, K. Suzuki, H. Murakoshi, R. S. Kasai, J. Kondo & T. Fujiwara (2005) "Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: High-speed single-molecule tracking of membrane molecules," Annu. Rev. Biophys. Biomol. Struct. 34: 351-378.
R. G. Parton, M. Hanzal-Bayer & J. F. Hancock (2006) "Biogenesis of caveolae: a structural model for caveolin-induced domain formation," J. Cell Sci. 119: 787-796.
T. J. McIntosh & S. A. Simon (2006) "Roles of bilayer material properties in function and distribution of membrane proteins," Annu. Rev. Biophys. Biomol. Struct. 35: 177-198.
J. P. DiNitto & D. G. Lambright (2006) "Membrane and juxtamembrane targeting by PH and PTB domains," 1761: 850-867.
F. M. Goñi & A. Alonso (2006) "Biophysics of sphingolipids I. Membrane properties of sphingosine, ceramides and other simple sphingolipids," Biochim. Biophys. Acta 1758: 1902-1921.
B. Ramstedt & J. P. Slotte (2006) "Sphingolipids and the formation of sterol-enriched ordered membrane domains," Biochim. Biophysics. Acta 1758: 1945-1956.
Potential Test Questions:
1.a. Draw the structure of the phospholipid molecule phosphatidyl
inositol. List (by name only) four compounds or groups that may substitute for
inositol in other glycerophospholipids. What gives a glycerophospholipid like phosphatidyl
inositol its amphipathic character?
b. What type of modification to phosphatidylinositol makes it able to bind a protein with a pleckstrin homology domain to the surface of a membrane?
2.a. What distinguishes an integral protein from a
peripheral membrane protein? Describe and explain what treatment may be required
to extract an integral protein from a membrane and maintain it in solution.
b. Describe the structural motif that is most common in integral membrane proteins. Explain how this structure is ideally suited for a transmembrane segment. Describe and explain the commonly observed distribution of specific amino acid types along the bilayer-spanning protein segment.
3.a. How is a hydropathy plot carried out? Explain
what conclusions can be drawn from such a plot.
b. Sketch hydropathy plots for proteins with either two or three transmembrane a-helices. For each of these proteins, draw a cartoon showing the predicted location of domains within and outside of the lipid bilayer, including locations of N-terminal and C-terminal domains. Briefly describe two ways in which the predicted location of these domains might be confirmed.
Studio Exercise - Hydropathy PlotThe primary sequence for the erythrocyte integral membrane protein glycophorin is found in the Excel worksheet linked below (and in Fig. 12-21 p. 397). Engleman-Steitz-Goldman estimates of the free energy associated with transfer of each type of amino acid R-group from oil to water, in kJ/mol, are listed below. Generate your own hydropathy plot comparable to that shown in Fig. 12-22 on p. 397.
Excel Worksheet (click here)
Be prepared to answer and explain the following:
DG for transferring amino acid side chains in a-helical polypeptides from oil to water, in kJ/mol:
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