Wiley-VCH - Books | August 2005 | Protein-Lipid Interactions

	Books \| August 2005 \| Protein-Lipid Interactions \| Table of contents

Books

	Just published
	Title search
	Featured sites
	Entertainment

Journals

Electronic Media

	Contents


	Preface	VII
	List of Contributors	XIX
Part 1	How Lipids Shape Proteins
1	Lipid Bilayers, Translocons and the Shaping of Polypeptide Structure Stephen H. White, Tara Hessa, and Gunnar von Heijne	3
1.1	Introduction	3
1.2	Membrane Proteins: Intrinsic Interactions	5
1.2.1	Physical Determinants of Membrane Protein Stability: The Bilayer Milieu	5
1.2.2	Physical Determinants of Membrane Protein Stability: Energetics of Peptides in Bilayers	9
1.2.3	Physical Determinants of Membrane Protein Stability: Helix--Helix Interactions in Bilayers	13
1.3	Membrane Proteins: Formative Interactions	14
1.3.1	Connecting Translocon-assisted Folding to Physical Hydrophobicity Scales: The Interfacial Connection	14
1.3.2	Connecting Translocon-assisted Folding to Physical Hydrophobicity Scales: Transmembrane Insertion of Helices	16
1.4	Perspectives	21
	References	22
2	Folding and Stability of Monomeric -Barrel Membrane Proteins Jörg H. Kleinschmidt	27
2.1	Introduction	27
2.2	Stability of -Barrel Membrane Proteins	29
2.2.1	Thermodynamic Stability of FepA in Detergent Micelles	29
2.2.2	Thermodynamic Stability of OmpA in Phospholipids Bilayers	30
2.2.3	Thermal Stability of FhuA in Detergent Micelles	31
2.3	Insertion and Folding of Transmembrane -Barrel Proteins	32
2.3.1	Insertion and Folding of -Barrel Membrane Proteins in Micelles	32
2.3.2	Oriented Insertion and Folding into Phospholipid Bilayers	32
2.3.3	Assemblies of Amphiphiles Induce Structure Formation in -Barrel Membrane Proteins	33
2.3.4	Electrophoresis as a Tool to Monitor Insertion and Folding of -Barrel Membrane Proteins	34
2.3.5	pH and Lipid Headgroup Dependence of the Folding of -Barrel Membrane Proteins	35
2.4	Kinetics of Membrane Protein Folding	35
2.4.1	Rate Law for -Barrel Membrane Protein Folding and Lipid Acyl Chain Length Dependence	35
2.4.2	Synchronized Kinetics of Secondary and Tertiary Structure Formation of the -Barrel OmpA	36
2.4.3	Interaction of OmpA with the Lipid Bilayer is Faster than the Formation of Folded OmpA	36
2.5	Folding Mechanism of the -Barrel of OmpA into DOPC Bilayers	37
2.5.1	Multistep Folding Kinetics and Temperature Dependence of OmpA Folding	37
2.5.2	Characterization of Folding Intermediates by Fluorescence Quenching	38
2.5.3	The -Barrel Domain of OmpA Folds and Inserts by a Concerted Mechanism	40
2.6	Protein--Lipid Interactions at the Interface of -Barrel Membrane Proteins	42
2.6.1	Stoichiometry of the Lipid--Protein Interface	42
2.6.2	Lipid Selectivity of -Barrel Membrane Proteins	42
2.7	Orientation of -Barrel Membrane Proteins in Lipid Bilayers	43
2.7.1	Lipid Dependence of the -Barrel Orientation Relative to the Membrane	43
2.7.2	Inclination of the -Strands Relative to the -Barrel Axis in Lipid Bilayers	44
2.7.3	Hydrophobic Matching of the -Barrel and the Lipid Bilayer	44
2.8	In vivo Requirements for the Folding of OMPs	45
2.8.1	Amino Acid Sequence Constraints for OmpA Folding in vivo	45
2.8.2	Periplasmic Chaperones	45
2.8.3	Insertion and Folding of the -Barrel OmpA is Assisted by Skp and LPS	46
2.8.4	Role of Omp85 in Targeting or Assembly of -Barrel Membrane Proteins	48
2.9	Outlook	51
	References	52
3	A Paradigm of Membrane Protein Folding: Principles, Kinetics and Stability of Bacteriorhodopsin Folding Paula J. Booth	57
3.1	Introduction	57
3.2	Principles of Transmembrane -Helical Membrane Protein Folding: A Thermodynamic Model for Bacteriorhodopsin	59
3.3	Bacteriorhodopsin Stability	60
3.3.1	Side-chain Contributions to Helix Interactions and the Role of Pro	61
3.3.2	Helix-connecting Loops	62
3.4	Pulling the Protein Out of the Membrane	63
3.5	Bacteriorhodopsin Folding Kinetics	64
3.5.1	Cotranslational Insertion	65
3.5.2	Retinal Binding Studies to Apomembrane	65
3.5.3	Unfolding, Refolding and Kinetic Studies in vitro	67
3.6	Controlling Membrane Protein Folding	69
3.7	Conclusions	71
3.7.1	Summary of Bacteriorhodopsin Folding	71
3.7.2	Implications for Transmembrane -Helical Membrane Protein Folding	73
	References	75
4	Post-integration Misassembly of Membrane Proteins and Disease Charles R. Sanders	81
4.1	Introduction	81
4.2	A Given IMP May be Subject to Numerous Disease-linked Mutations	82
4.3	Ligand Rescue of Misassembly-prone Membrane Proteins: Implications	84
4.4	What IMP Properties Affect Folding Efficiency in the Cell?	87
4.5	Common Mutations in Transmembrane Domains That Lead to Misassembly and Disease	89
4.6	Correlating Biophysical, Cell-biological and Biomedical Measurements	90
	References	91
Part 2	How Proteins Shape Lipids
5	A Census of Ordered Lipids and Detergents in X-ray Crystal Structures of Integral Membrane Proteins Michael C. Wiener	97
5.1	Introduction	97
5.2	Results	98
5.3	Illustrative Examples of Selected Bound Lipids, Detergents and Related Molecules	103
5.3.1	Integral Membrane Protein Structures Contain Ordered Native Lipids	103
5.3.2	Structures of Lipids in Membrane Protein Co-crystals Differ from Those in Pure Lipid Crystals	107
5.3.3	Native Lipids can Stabilize and Preserve Protein--Protein Interfaces	108
5.3.4	Multiple Acyl Chain Conformations Exist for Efficient Packing with Protein Interfaces	108
5.3.5	Lipid Acyl Chains Interact Primarily with Aliphatic and Aromatic Amino Acid Side-chains	109
5.3.6	Unusual Lipid/Detergent Conformations Occur at the Protein--Lipid Interface	109
5.3.7	A Bilayer Structure is Present in Crystals Grown from the LCP	112
5.4	Conclusion	114
	References	115
6	Lipid and Detergent Interactions with Membrane Proteins Derived from Solution Nuclear Magnetic Resonance Ashish Arora	119
6.1	Introduction	119
6.2	Heteronuclear Solution NMR of Protein/Detergent Complexes	120
6.3	Choice of Detergents	122
6.4	Size and Shape of Pure Detergent Micelles and Detergent/Protein Complexes	124
6.5	Sample Preparation for Solution NMR Measurements	125
6.6	Protein/Detergent Interactions Monitored by NMR Spectroscopy	128
6.7	Dynamics and Conformational Transitions of Membrane Proteins in Detergent Micelles	130
6.8	MD Simulations of Protein/Detergent Complexes	131
6.9	Implications on the Structure and Function of Membrane Proteins in Biological Membranes	133
	References	134
Part 3	Membrane Penetration by Toxins
7	Lipid Interactions of -Helical Protein Toxins Gregor Anderluh and Jeremy H. Lakey	141
7.1	Introduction	141
7.1.1	The Two Secondary Structures Compared	141
7.1.2	Lessons from a Potassium Channel	145
7.2	Pore-forming Colicins	145
7.2.1	Outer Membrane Interactions	146
7.2.2	Colicin A Requires Acidic Lipids	147
7.2.3	The Open Channel	148
7.2.4	The Colicin--Phospholipid Complex	149
7.2.5	Other Similar Proteins	150
7.3	Actinoporins	151
7.3.1	Initial Lipid Binding	152
7.3.2	Helix Insertion	154
7.3.3	The Oligomeric Pore	155
7.4	Conclusion	156
	References	157
8	Membrane Recognition and Pore Formation by Bacterial Pore-forming Toxins Alejandro P. Heuck and Arthur E. Johnson	163
8.1	Introduction	163
8.2	Classification of Bacterial PFTs	163
8.2.1	-PFTs	164
8.2.2	-PFTs	166
8.3	A General Mechanism of Pore Formation?	166
8.4	Membrane Recognition	169
8.4.1	Recognition of Specific Membrane Lipids	170
8.4.2	Recognition of Membrane-anchored Proteins or Carbohydrates	172
8.4.3	The Role of Membrane Lipid Domains	173
8.5	Oligomerization on the Membrane Surface	175
8.5.1	Oligomerization Triggered by Lipid-induced Conformational Changes	176
8.5.2	Oligomerization Following Proteolytic Activation of Toxins	178
8.6	Membrane Penetration and Pore Formation	179
8.7	Unresolved Issues	181
	References	183
9	Mechanism of Membrane Permeation and Pore Formation by Antimicrobial Peptides Yechiel Shai	187
9.1	Introduction	187
9.2	The Cell Membrane is the Major Binding Site for Most Cationic Antimicrobial Peptides	188
9.2.1	Non-receptor-mediated Interaction of Antimicrobial Peptides with their Target Cells	189
9.2.2	A Receptor-mediated Interaction of Antimicrobial Peptides with their Target Cells	191
9.3	Parameters Involved in the Selection of Target Cells by Antimicrobial Peptides	192
9.3.1	The Role of the Composition of the Cell Wall and the Cytoplasmic Membrane	193
9.3.2	The Role of the Peptide Chain and Its Organization	194
9.3.2.1	The Extent of Hydrophobicity and Distribution of Positively-charged Amino Acids Along the Peptide Chain	194
9.3.2.2	The Stability of the Amphipathic Structure	194
9.3.2.3	The Ability of a Peptide to Self-associate in Solution and/or in Membranes	195
9.3.2.4	Fatty Acid Modification can Compensate for the Hydrophobicity and Amphipathicity of the Peptide Chain	200
9.4	The Lethal Event Caused by Antimicrobial Peptides	201
9.5	How do Antimicrobial Peptides Damage the Integrity of the Target Cell Membrane?	202
9.5.1	Membrane-imposed Amphipathic Structure	202
9.5.2	Molecular Mechanisms of Membrane Permeation	204
9.5.2.1	Pore Formation via the Barrel--Stave Model	204
9.5.2.2	The Carpet Model	205
9.5.3	The Molecular Architecture of the Permeation Pathway	208
9.5.3.1	Toroidal Pores	208
9.5.3.2	Channel Aggregates/Hydrophobic Pores	208
9.6	Summary and Conclusions	209
	References	210
Part 4	Mechanisms of Membrane Fusion
10	Cell Fusion in Development and Disease Benjamin Podbilewicz and Leonid V. Chernomordik	221
10.1	Introduction	221
10.2	Developmental Cell Fusion for Health	221
10.2.1	Muscles	222
10.2.1.1	Vertebrates	222
10.2.1.2	Drosophila	223
10.2.2	C. elegans	226
10.2.2.1	Epithelial Cell Fusion Assay in C. elegans	227
10.2.2.2	Control of Cell Fusion	227
10.2.2.3	Developmental Genetics of Cell Fusion in C. elegans	227
10.2.2.4	eff-1 Mutant Epidermal Cells do not Initiate Cell Membrane Fusion	228
10.2.2.5	eff-1-mediated Cell Fusion is Essential for Healthy Organogenesis	228
10.2.2.6	eff-1 Encodes Novel Type I Membrane and Secreted Proteins	230
10.2.2.7	eff-1 is Highly Expressed in Epidermal Cells Ready to Fuse	230
10.2.2.8	eff-1 is Sufficient for Cell Membrane Fusion in vivo	230
10.2.2.9	Tissue-specific Fusogenic Activity of eff-1 in Pharyngeal Muscles	231
10.2.3	Comparison between Cell Fusion in a Worm, a Fly and Vertebrates	231
10.3	Cell Fusion in Diseases	233
10.3.1	Cell Fusion Mediated by Enveloped Viruses	233
10.3.1.1	Dissection of Viral Membrane Fusion	234
10.3.1.2	Initiation and Expansion of Membrane Fusion	234
10.3.1.3	Protein--Protein and Protein--Lipid Interactions in Membrane Fusion	235
10.3.1.4	The Role of Fusion Proteins Outside the Fusion Site	236
10.3.1.5	HA Insiders Initiate Hemifusion and HA Outsiders Expand Fusion Pores	236
10.3.1.6	Models for Final Expansion of Fusion Pores	237
10.4	Dissection of Developmental Fusion Based on Viral Fusion Analogies	239
10.4.1	Activation of a Developmental Fusogen	239
10.4.2	Dissection of Developmental Cell Fusion	239
10.4.3	Direct Cell Fusion Promotion or Indirect Relaxation of Fusion Blocks	240
10.5	Concluding Remarks	240
	References	241
11	Molecular Mechanisms of Intracellular Membrane Fusion Olga Vites and Reinhard Jahn	245
11.1	Introduction	245
11.2	Intracellular Fusion Reactions -- An Overview	246
11.3	Tethering and Docking	247
11.4	SNARE Proteins -- The Fusion Catalysts?	249
11.4.1	Assembly--Disassembly Cycle of SNARE Proteins	249
11.4.2	N-terminal Domains of SNAREs -- Recruiting Proteins or Regulating SNARE Function?	251
11.4.3	Zippering Model for SNARE-mediated Membrane Fusion	252
11.4.4	Trans-complexes -- Intermediates in the Fusion Pathway?	253
11.4.5	Acceptor Complexes, Topology and Specificity	256
11.4.5.1	SNARE Acceptor Complexes	256
11.4.5.2	Topology of SNAREs	257
11.4.5.3	Specificity of SNAREs	258
11.4.6	Challenges of the SNARE Hypothesis	259
11.4.6.1	Persistence of Fusion in Spite of SNARE Deletions	260
11.4.6.2	Late-acting Factors Uncovered in Yeast Vacuolar Fusion	260
11.4.6.3	Exocytosis of Cortical Granules in Sea Urchin Oocytes	262
11.5	SM Proteins and Other Regulators	262
11.5.1	SM Proteins	263
11.6	Fusion Pores	264
11.6.1	Measuring Fusion Pore Opening and Closure	265
11.6.2	The Role of Proteins in Controlling Fusion Pore Opening	266
11.7	Concluding Remarks	267
	List of Abbreviations	267
	References	268
12	Interplay of Proteins and Lipids in Virus Entry by Membrane Fusion Alex L. Lai, Yinling Li, and Lukas K. Tamm	279
12.1	Introduction	279
12.2	Fusion of Pure Lipid Bilayers	281
12.3	Viral Protein Sequences that Mediate Lipid Bilayer Fusion	284
12.3.1	Fusion Peptides	284
12.3.2	Transmembrane Domains	285
12.3.3	Other Regions of the Fusion Protein	285
12.4	Interactions of Fusion Peptides with Lipid Bilayers	286
12.4.1	HIV Fusion Peptide--Bilayer Interactions	287
12.4.2	Influenza Fusion Peptide Structure	288
12.4.3	Influenza Fusion Peptide Mutants	290
12.4.4	Binding of Fusion Peptides to Lipid Bilayers	290
12.4.5	Sendai, Measles and Ebola Fusion Peptide--Bilayer Interactions	290
12.4.6	Perturbation of Bilayer Structure by Fusion Peptides	291
12.5	Interactions of Transmembrane Domains with Lipid Bilayers	292
12.6	Structure--Function (Fusion) Relationships of Membrane-interactive Viral Fusion Protein Domains	294
12.6.1	Fusion Peptide Mutants	294
12.6.2	Transmembrane Domain Mutants	295
12.7	Possible Mechanisms for Initiating the Formation of Viral Fusion Pores	296
	References	300
Part 5	Cholesterol, Lipid Rafts, and Protein Sorting
13	Protein--Lipid Interactions in the Formation of Raft Microdomains in Biological Membranes Akihiro Kusumi, Kenichi Suzuki, Junko Kondo, Nobuhiro Morone, and Yasuhiro Umemura	307
13.1	Many Plasma Membrane Functions are Mediated by Molecular Complexes, Microdomains and Membrane Skeleton-based Compartments	307
13.2	Timescales, Please!	309
13.3	Four Types of Membrane Domains	310
13.4	The Cell Membrane is a Two-dimensional Non-ideal Liquid Containing Dynamic Structures on Various Time-Space Scales	314
13.5	A Definition of Raft Domains	315
13.6	The Original Raft Hypothesis	316
13.7	Are there Raft Domains in Steady-state Cells in the Absence of Extracellular Stimulation?	316
13.7.1	Standard Immunofluorescence or Immunoelectron Microscopy Failed to Detect Raft-like Domains in the Plasma Membrane of Steady-state Cells	317
13.7.2	The Recovery of a Molecule in Detergent-resistant Membrane (DRM) Fractions Might Infer its Raft Association in the Cell Membrane, but the Relationship between DRM Fractions and Raft Domains is Complicated	317
13.7.3	The Size of Rafts in Plasma Membranes of Steady-state Cells may be 10 nm or Less	319
13.7.4	Mushroom Model for the Steady-state Raft	322
13.8	Stabilized Rafts Induced by Protein Clustering in Plasma and Golgi Membranes	324
13.8.1	Clustering of Raft Molecules by Ligand Binding or Crosslinking Induces Stabilized Rafts (Receptor-cluster Rafts)	324
13.8.2	How can Raft Molecule Clustering Induce Stabilized Rafts?	324
13.9	Can Receptor-cluster Rafts Work as Platforms to Facilitate the Assembly of Raftophilic Molecules?	326
13.9.1	Benchmarks for Experiments Examining the Colocalization of Raftophilic Molecules	326
13.9.2	Simultaneous Crosslinking of Two GPI-anchored Receptors	327
13.9.3	Sequential Crosslinking of One Species of GPI-anchored Receptors Followed by Crosslinking of a Second Species without Fixation	328
13.9.4	Examination of the Recruitment of Non-crosslinked Second Raftophilic Molecules to Crosslinked GPI-anchored Receptor Clusters	328
13.9.5	Difficulty in Colocalization Experiments using Raftophilic Molecules: Low Levels of Colocalization and Quantitative Reproducibility Due to Sensitivity to Subtle Differences in Experimental Conditions and Protocols	329
13.10	Timescales Again! Transient Colocalization of Raftophilic Molecules	329
13.11	Modified Raft Hypothesis	331
	References	332
14	Protein and Lipid Partitioning in Locally Heterogeneous Model Membranes Petra Schwille, Nicoletta Kahya, and Kirsten Bacia	337
14.1	Introduction: Why Should We Use Simple Model Membranes to Gain Insight into Complex Membrane Organization?	337
14.1.1	Relation of Domain Structure to a Biological Function	337
14.1.2	An Accessible Detection Method	338
14.1.3	The Term Raft	338
14.2	Biomimetic Membranes	340
14.2.1	GUVs: Properties and Preparation	342
14.3	Methods of Investigation of Domain Formation in Biomimetic Membranes	343
14.3.1	Electron Microscopy	343
14.3.2	Atomic Force Microscopy (AFM)	343
14.3.3	Near-field Scanning Optical Microscopy (NSOM)	344
14.3.4	Fluorescence Imaging (Confocal, Multi-photon)	344
14.3.5	Fluorescence Photobleaching Recovery (FPR) or Fluorescence Recovery after Photobleaching (FRAP)	344
14.3.6	Single Particle Tracking (SPT)	344
14.3.7	Fluorescence Correlation Spectroscopy (FCS)	345
14.4	Lipid Domain Assembly in GUVs	345
14.4.1	Phase Separation	345
14.4.1.1	Can Cellular Membrane Domains be Regarded as Phase Domains?	345
14.4.1.2	Properties of Lipid Bilayer Phases	347
14.4.1.3	Co-existence of Lipid Bilayer Phases	348
14.4.1.4	Lipid Phase Diagrams	348
14.4.2	Binary Lipid Systems	348
14.4.3	Ternary Lipid Systems	351
14.4.4	Effect of Sterols on Lipid Segregation	353
14.4.5	Lipid Dynamics in Domain-exhibiting GUVs	354
14.4.5.1	Fluidizing Effect of Cholesterol for High-Tm Lipids	355
14.4.5.2	Condensing Effect of Cholesterol for Low-Tm Lipids	356
14.5	Spatial Organization and Dynamics of Membrane Proteins in GUVs	357
14.6	From Model to Cellular Membranes	358
14.6.1	Model Membranes Constitute Test Systems for Developing New and Improving Existing Detection Techniques	358
14.6.2	Direct Comparison Between Results Obtained on Model and Native Membranes	361
14.6.3	Model Membranes Demonstrate What Structures Can be Potentially Formed by Lipids and Proteins, and Suggest Mechanisms for Fulfilling in vivo Functions	361
	References	362
Part 6	Targeting of Extrinsic Membrane Protein Modules to Membranes and Signal Transduction
15	In vitro and Cellular Membrane-binding Mechanisms of Membrane-targeting Domains Wonhwa Cho and Robert V. Stahelin	369
15.1	Introduction	369
15.2	Membrane Interactions of Membrane-targeting Domains	370
15.2.1	Interfacial Location of Membrane-targeting Domains	370
15.2.2	Energetics and Kinetics of Membrane--Protein Interactions	371
15.3	C1 Domains	373
15.3.1	Occurrence and Structure	373
15.3.2	Lipid Specificity	374
15.3.3	Membrane-binding Mechanisms	374
15.3.4	Subcellular Localization	375
15.4	C2 Domains	376
15.4.1	Occurrence and Structure	376
15.4.2	Lipid Specificity	376
15.4.3	Membrane Binding Mechanisms	377
15.4.4	Subcellular Localization	378
15.5	PH Domains	378
15.5.1	Occurrence, Structure and Lipid Specificity	378
15.5.2	Membrane-binding Mechanisms	380
15.5.3	Subcellular Localization	380
15.6	FYVE Domains	380
15.6.1	Occurrence, Structure and Lipid Specificity	380
15.6.2	Membrane-binding Mechanism	382
15.6.3	Subcellular Localization	383
15.7	PX Domains	384
15.7.1	Occurrence, Structure and Lipid Specificity	384
15.7.2	Membrane-binding Mechanism	385
15.7.3	Subcellular Localization	385
15.8	ENTH and ANTH Domains	387
15.8.1	Occurrence, Structure and Lipid Specificity	387
15.8.2	Membrane-binding Mechanism	387
15.9	BAR Domains	389
15.10	FERM Domains	390
15.11	Tubby Domains	391
15.12	Other Phosphoinositide-binding Domains	391
15.13	Perspectives	392
	References	393
16	Structure and Interactions of C2 Domains at Membrane Surfaces David S. Cafiso	403
16.1	Introduction	403
16.2	C2 Domains: CaŽ2+-dependent and CaŽ2+-independent Membrane Binding	404
16.3	What Drives Membrane Targeting of C2 Domains?	405
16.4	Electrostatic Binding of Simple Linear Protein Motifs	406
16.5	The Results of Electrostatic Calculations on C2 Domains	408
16.6	Determining the Interactions and Positions of C2 Domains	410
16.6.1	Site-directed Mutagenesis	410
16.6.2	Chemical Labeling	410
16.6.3	Fluorescence	411
16.6.4	Site-directed Spin Labeling (SDSL) to Determine C2 Domain Orientation	411
16.7	Proteins with Multiple C2 Domains	416
16.8	Interactions of Phosphoinositides with C2 Domains	417
	References	418
17	Structural Mechanisms of Allosteric Regulation by Membrane-binding Domains Bertram Canagarajah, William J. Smith, and James H. Hurley	423
17.1	Introduction	423
17.2	How Membranes and PH Domains Regulate Rho Family-specific Guanine Nucleotide Exchange Factors (GEFs)	424
17.2.1	DH and PH Domain Rho GEFs	425
17.2.2	Regulation of GEF Activity by PH Domains	425
17.3	Regulation of G-protein Receptor Kinase (GRK) 2 Activity by Lipids and the Gbc Subunit at the Membrane	429
17.4	Lipid Activation of Rac-GAP Activity: b2-Chimaerin	432
17.4.1	The C1 Domain of b2-Chimaerin is Buried	432
17.4.2	Mechanism of Allosteric Rac-GTPase Activation by the C1 Domain	434
	References	435
	Subject Index	437

	Order
	Online book
	Table of contents
	Short description
	Detailed description
	Reviews
	Author information
	Author affiliation


	Encyclopedia of Industrial Biotechnology. Bioprocess, Bioseparation, and Cell Technology 7 Volume Set Adipose Tissue in Health and Disease Quantum Biochemistry
	[more >>]


	Archiv der Pharmazie European Journal of Lipid Science and Technology Chemistry & Biodiversity
[more>>]


	Weiner, Irving B. / Craighead, W. Edward The Corsini Encyclopedia of Psychology 495.- Euro valid until 3 May 2010
	[more offers >>]

Tell a friend RSS Feeds Print-Version

©2010 Wiley-VCH Verlag GmbH & Co. KGaA - Provider
http://www.wiley-vch.de - mailto: info@wiley-vch.de
Data Protection