Protein-lipid interactions

목차 (Table of Contents)

• CONTENTS
• Preface = ⅴ
• List of Contributors = ⅶ
• Chapter 1. Protein―lipid interactions and membrane heterogeneity / Ole G. Mouritsen ; Rodney L. Biltonen = 1
• Abbreviations = 1
• 1. Perspectives and overview = 1
• 1.1. Lipids, proteins, and the biological membrane = 1
• 1.2. Phase transitions and membrane heterogeneity = 3
• 2. Membrane heterogeneity = 4
• 2.1. Static membrane heterogeneity = 4
• 2.2. Dynamic membrane heterogeneity = 4
• 3. Evidence of heterogeneity in lipid bilayers = 6
• 3.1. What can thermodynamics tell us? = 6
• 3.1.1. Differential scanning calorimetry = 7
• 3.1.1.1. A simple two-state model = 8
• 3.1.2. Volume perturbation caiorimetry = 12
• 3.1.3. The effect of anesthetics on the gel-to-fluid transition = 16
• 3.2. What can microscopic modelling tell us? = 16
• 4. Effects of proteins on membrane heterogeneity = 19
• 4.1. Perturbation of lipid acyl-chain structure by integral membrane proteins = 20
• 4.2. Lateral distribution of proteins in membranes = 21
• 4.3. Compositional membrane heterogeneity induced by protein-lipid interactons: lipid enrichment and selectivity = 25
• 5. The effect of lipid structure on protenin state and functions = 27
• 6. Lipid microheterogeneity and the activation of phospholipase A $$A_2$$ = 29
• 7. Effects of drugs on protein-lipid interactions and membrane heterogeneity = 33
• References = 34
• Chapter 2. The nature of the lipid―protein interface and the influence of protein structure on protein-lipid interactions Derek Marsh = 41
• 1. Introduction = 41
• 2. Molecular modelling and crystal structures = 43
• 3. Lipid chain ordering: NMR and ESR results = 46
• 4. Hydrophobia matching, membrane thickness and protein secondary structure = 47
• 5. Protein conformation and lipid-protein stoichiometry = 48
• 6. Protein secondary structure and lipid-protein interactions = 53
• 7. Selectivity of lipid-protein interaction = 55
• 8. Protein sequence and lipid selectivity = 57
• 9. Conclusions = 63
• References = 64
• Chapter 3. Cooperative regulation of membrane enzymes by lipids / H. Sandermann Jr. ; T.M. Duncan ; J.O. Mclntyre ; S. Fleischer = 67
• Abbreviations = 67
• 1. Introduction = 67
• 2. Lipid specificity = 69
• 3. Case studies = 70
• 3.1. Cardiolipin synthase = 70
• 3.2. Diacylglycerol kinase = 70
• 3.2.1. Lipid specincity = 70
• 3.2.2. Kinetic cooperativity = 72
• 3.3. R-3-Hydroxybutyrate dehydrogenase = 72
• 3.3.1. Lipid specificity = 72
• 3.3.2. Kinetic cooperativity = 73
• 3.3.3. Basis of the role for phosphatidylcholine = 75
• 3.4. Protein Kinase C = 75
• 3.4.1. Background = 75
• 3.4.2. Proposed mechanisms = 76
• 3.4.3. Trapping model = 77
• 3.4.4. Electrostatic mechanism = 79
• 3.5. Pyruvate oxidase = 79
• 4. Conclusions = 82
• References = 83
• Chapter 4. Lipid―protein interaction in a biological membrane: Effect of cholesterol and acyl chain degree of unsaturation / Celina E. Castuma ; M. Teresa Lamy-Freund ; Rudolfo R. Brenner ; Shirley Schreier = 87
• Abbreviations = 87
• 1. Introduction = 87
• 2. Effect of cholesterol and acyl chain degree of unsaturation on the kinetic properties of UDP-glucuronyI transferase = 88
• 2.1. Effect of in vivo modification of cholesterol content = 89
• 2.2. Effect of in vitro modification of cholesterol content = 91
• 2.3. Effect of in vivo modification of acyi chain degree of unsaturation = 91
• 2.4. Significance of the kinetic data = 94
• 3. Fluorescence studies ofbilayer properties in normal and modified microsomes, and in extracted lipids = 95
• 3.1. Spectral behaviour of fluorescent probes = 95
• 3.2. Significance of the'fluorescence data = 98
• 4. Spin label study of the effect of cholesterol on lipid-protein interactions in microsomal membranes = 98
• 4.1. Spectral behaviour of spin label probes = 98
• 4.2. Significance of spin label data = 102
• 5. Possible models for the effect of cholesterol and acyl chain unsaturation on lipid-protein interaction = 102
• 6. Concluding remarks = 103
• Acknowledgements = 104
• References = 104
• Chapter 5. Lipid―peptide interactions in model systems: Membrane insertion and translocation ofpeptides / A.I.P.M. de Kroon ; J.de Gier ; B. de Kruijff = 107
• Abbreviations = 107
• 1. Introduction = 107
• 2. Membrane affinity and topology of the peptides = 109
• 3. Consequences of peptide insertion for structural and dynamic properties of the phospholipid bilayer = 112
• 4. Peptide translocation across a phospholipid bilayer and ion gradients = 115
• 5. Biologically active peptides = 120
• 6. Conclusions = 123
• Acknowledgements = 124
• References = 124
• Chapter 6. Protein―lipid interactions with peripheral membrane proteins Mantripragada B. Sankaram and Derek Marsh = 127
• Abbreviations = 127
• 1. Introduction = 128
• 2. Binding requirements／modes = 129
• 2.1. Binding = 129
• 2.2. Functional implications = 130
• 3. Surface electrostatics = 131
• 3.1. Binding isotherms = 131
• 3.2. Strength of binding = 133
• 3.3. Ionic strength and pH dependence = 135
• 4. Surface dehydration = 137
• 4.1. Interfacial pK = 137
• 4.2. Fluorescence isotope effects = 137
• 5. Membrane penetration = 138
• 5.1. Electron spin resonance = 139
• 5.2. Photochemical crosslinking = 140
• 5.3. Tryptophan fluorescence = 141
• 6. Lipid selectivity = 142
• 6.1. Selectivity sequence = 142
• 6.2. Functional implications of specificity = 145
• 7. Phase separation／lipid polymororphism = 146
• 7.1. Phase separation = 146
• 7.2. Lipid polymorphism = 146
• 8. Covalently linked acyl chains = 148
• 8.1. Membrane attachment = 150
• 8.2. Protein-protein interactions = 151
• 9. Protein conformation = 151
• 9.1. Circular dichroism = 151
• 9.2. Fourier transform infrared spectroscopy = 153
• 9.3. Nuclear magnetic resonance = 153
• 10. Peripheral protein-integral protein interactions = 154
• 10.1. Specific interactions = 155
• 10.2. Transmembrane signalling = 156
• 11. Conclusions = 158
• Acknowledgements = 158
• References = 158
• Chapter 7. Genetic studies on the functions of membrane―forming phospholipids / T.P. McGee ; M.K.Y. Fung ; V.A. Bankaitis = 163
• Abbreviations = 163
• 1. Introduction = 163
• 2. Genetics of phospholipid biosynthesis = 165
• 2.1. Phospholipid synthesis in Escherichia coli = 165
• 2.2. Phospholipid biosynthesis in yeast = 167
• 3. The genetic case for lipids as cofactors = 170
• 4. Functions of acidic phospholipids in E. coli = 171
• 4.1. Acidic phospholipids and secretion = 171
• 4.2. Cardiolipin and DNA replication = 173
• 5. Functions of phospholipids in eukaryotes = 174
• 5.1. The phospholipid composition of the Golgi is critical to secretory function = 174
• 5.1.1. Identification of the SEC14p and the connection to phospholipids = 174
• 5.1.2. Testing the PI / PC ratio hypothesis = 177
• 5.1.3.Genetic distinctions between the CDP-choline pathway and the PE methylation pathway = 178
• 5.1.4. Why phospholipids and Golgi function? = 181
• 5.2. Fatty acid unsaturation and mitochondrial inheritance = 185
• 5.3. PIasmalogen synthesis and peroxisome biogenesis = 186
• 6. Summary = 187
• References = 187
• Chapter 8. Lipid―protein interactions involved in bacteriophage M13 infection / Marcus A. Hemminga ; Johan C. Sanders ; Cor J.A.M Wolfs ; Ruud B. Spruijt = 191
• Abbreviations = 191
• 1. Introduction = 191
• 2. The M13 virion and its reproductive life cycle = 192
• 2.1. M13 bacteriophage = 192
• 2.2. Reproductive cycle = 192
• 2.3. Biological questions = 194
• 3. The major coat protein during the infection process = 195
• 3.1. M13 major coat protein = 195
• 3.2. Effects of phospholipids = 195
• 4. Reconstitution of M13 coatprotein = 196
• 4.1. General principles = 196
• 4.2. Basic conformations of transmembrane domains = 196
• 5. The in vitro membrane-bound state of M13 coat protein = 198
• 5.1. The $$\alpha$$-helican and $$\beta$$-polymeric state = 198
• 5.2. Putative in vivo state of M13 coat protein = 198
• 5.3. Reconstitution procedures = 199
• 6. The coat protein structure = 200
• 6.1. Secondary structure - transmembrane helix = 200
• 6.2. Secondary structure - the terminal parts = 201
• 6.3. The N-tcrminal helix = 201
• 6.4. Molecular dynamics = 202
• 7. Lipid order and dynamics in reconstituted systems = 203
• 7.1. Protein packing in the bilayer = 203
• 7.2. Protein aggregation = 204
• 7.3. Model for protein-lipid interaction = 204
• 7.4. The phospholipid headgroup region = 206
• 7.5. Dynamic protein-lipid network = 207
• 8. Concluding remarks = 208
• Acknowledgements = 209
• References = 209
• Chapter 9. Functional aspects of acetylcholine receptor―lipid interactions / Saffron E. Rankin ; Douglas E. Raines ; Lauraine A. Dalton ; Keith W. Miller = 213
• Abbreviations = 213
• 1. Introduction = 213
• 1.1. Acetylcholine receptor states = 214
• 1.2. Acetylcholine receptor structure = 215
• 2. Information from the lipid-protein interface = 218
• 2.1. Spectroscopic studies of the lipid-protein interface of the nAcChoR = 218
• 2.2. Axial orientation of the transmembrane helices within the bilayer = 220
• 3. The lipid environment of the nAcChoR = 221
• 4. Towards more definitive kinetics of reconstituted systems = 224
• 4.1. The framework for a new approach = 224
• 4.2. The limitations of current work = 224
• 4.3. Introduction of new probes = 226
• 4.4. Other structural approaches = 227
• References = 228
• Chapter 10.The lipid annulus of the nicotinic acetylcholine receptor as a locus of structural-functional interactions / F.J. Barrantes = 231
• 1. Introduction = 231
• 2. AChR ligand sites = 231
• 3. Topographical relationship between AChR and membrane lipids: From structural data to structural-functional correlations = 233
• 4. Structural asymmetry of the AChR-rich membrane. I. The annulus = 239
• 4.1. Early data on immobilized tipid in AChR-rich membranes = 239
• 4.2. Quantitation of annular lipid = 240
• 4.3. Non-annular sites = 244
• 5. Structural asymmetry of the AChR-rich membrane. II. The two leaflets of the bilayer = 244
• 6. Testing the influence of tipid on AChR in situ = 245
• 6.1. Phospholipid polar headgroup substitution = 246
• 6.2. Cholesterol = 247
• 6.3. Fatty acids = 249
• 7. Concluding remarks = 252
• Acknowledgements = 252
• References = 252
• Chapter 11. The ($$Ca^{2+}$$-$$Mg^{2+}$$)-ATPase and other membrane Proteins: what reconstitution tells us about the biological membrane / Anthony G. Lee ; J. Malcolm East = 259
• Abbreviations = 259
• 1. Introduction = 259
• 2. Why should phospholipid structure affect the function of membrane proteins = 263
• 2.1. The membrane and the cell = 263
• 2.2. Selectivity in phospholipid-protein interactions = 264
• 2.3. Effects on enzyme function = 269
• 2.3.1. General principles = 269
• 2.3.2. The ($$Ca^{2+}$$-$$Mg^{2+}$$)-ATPase = 277
• 2.3.3. Other ATPases = 288
• 2.3.4. Other systems = 289
• 2.4. Diffusion in the membrane = 291
• 3. Extrapolation to the biological membrane = 293
• Acknowledgements = 295
• References = 295
• Chapter 12. The functional effects of protein and lipid dynamics in sarcoplasmic reticulum / David D. Thomas ; James E. Mahaney = 301
• Abbreviations = 301
• 1. Introduction = 301
• 2. Spectroscopic methods for studying membrane molecular dynamics = 303
• 2.1. Electron paramagnetic resonance = 303
• 2.1.1. Conventional EPR = 303
• 2.1.2. Saturation transfer EPR = 305
• 2.2. Time-resolved fluorescence and phosphorescence anisotropy = 306
• 2.3. Relationship between lipid fluidity and-protein mobility = 307
• 3. Correlation of molecular dynamics with Ca-ATPase function = 309
• 3.1. Temperature variation = 309
• 3.1.1. EPR studies of temperature effects in SR = 310
• 3.1.2. TPA analysis of temperature dependence in SR = 310
• 3.1.3. Effective temperature change = 311
• 3.2. Perturbation of lipid fluidity = 311
• 3.2.1. Decreased fluidity: Lipid substitution or delipidation = 311
• 3.2.2. Increased fluidity: Diethyl ether = 312
• 3.2.3. Variation of bilayer thickness = 312
• 3.3. Direct perturbation of protein-protein interactions = 313
• 3.3.1. Covalent cross-linking = 313
• 3.3.2. Peptide effects on protein-protein interactions = 313
• 3.4. Cardiac SR = 316
• 4. Conclusions = 318
• Acknowledgements = 319
• References = 319
• Chapter 13. Infrared spectroscopic studies of lipid―protein interactions in membranes / Jos$$\acute e$$ Luis R. Arrondo ; F$$\acute e$$lix M. Go$$\tilde n$$i = 321
• Abbreviations = 321
• 1. The problem = 321
• 2. The technique = 323
• 2.1. Dispersive versus FT-IR spectroscopy = 323
• 2.2. Data processing = 326
• 2.2.1. Fourier deconvolution and LOMEP = 326
• 2.2.2. Derivation = 328
• 2.2.3. Differential spectroscopy = 329
• 2.3. Technical improvements desired and foreseen = 330
• 3. Recent studies = 331
• 3.1. Lipid components = 331
• 3.1.1. The acyi chain region = 333
• 3.1.2. The interfacial region = 335
• 3.1.3. The phosphate group region = 336
• 3.2. Protein structure = 336
• 3.2.1. Assignment of protein bands = 336
• 3.2.2. Quantification of protein secondary structure by FT-IR. spectroscopy = 338
• 3.3. How proteins influence lipid structure = 339
• 3.4. How lipids influence protein structure = 342
• 4. Looking into the future = 344
• Acknowledgments = 345
• References = 345
• Chapter 14. Lipid―protein interactions in controlled membrane, protein array and crystal formation / A. Watts, C. V$$\acute e$$nien-bryan ; M. Sami ; C. Whiteway ; J. Boulter ; B. Sternberg = 351
• 1. Introduction = 351
• 2. Possible involvement of lipids in the formation of arrays or crystals of membrane proteins = 352
• 3. Two-dimensional protein arrays = 355
• 3.1. Bacterial porins = 355
• 3.2. Photosystem I reaction centre = 357
• 3.3. Light-harvesting chlorophyll a／b-protein complex, LHC-II = 358
• 3.4. $$NA^+$$,$$K^+$$-ATPase = 359
• 3.5. Bacteriorhodopsin = 360
• 3.6. Other proteins = 361
• 3.7. Summary = 362
• 4. Three-dimensional crystallization of integral membrane proteins = 362
• 4.1. Porins = 363
• 4.2. Bacteriorhodopsin = 364
• 4.3. Band 3 = 365
• 4.4. Other proteins = 366
• 4.5. Summary = 367
• 5. Conclusion = 368
• Acknowledgements = 368
• References = 368
• Index = 371