Protein-lipid interactions [[electronic resource] ] : from membrane domains to cellular networks / / edited by Lukas K. Tamm |
Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2005 |
Descrizione fisica | 1 online resource (472 p.) |
Disciplina | 572.68 |
Altri autori (Persone) | TammLukas K |
Soggetto topico |
Membrane proteins
Lipoproteins Lipids Proteins Protein binding Membrane lipids |
Soggetto genere / forma | Electronic books. |
ISBN |
1-280-85408-1
9786610854080 3-527-60676-9 3-527-60699-8 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Protein-Lipid Interactions; Preface; Contents; List of Contributors; Part 1 How Lipids Shape Proteins; 1 Lipid Bilayers, Translocons and the Shaping of Polypeptide Structure; 1.1 Introduction; 1.2 Membrane Proteins: Intrinsic Interactions; 1.2.1 Physical Determinants of Membrane Protein Stability: The Bilayer Milieu; 1.2.2 Physical Determinants of Membrane Protein Stability: Energetics of Peptides in Bilayers; 1.2.3 Physical Determinants of Membrane Protein Stability: Helix-Helix Interactions in Bilayers; 1.3 Membrane Proteins: Formative Interactions
1.3.1 Connecting Translocon-assisted Folding to Physical Hydrophobicity Scales: The Interfacial Connection1.3.2 Connecting Translocon-assisted Folding to Physical Hydrophobicity Scales: Transmembrane Insertion of Helices; 1.4 Perspectives; References; 2 Folding and Stability of Monomeric β-Barrel Membrane Proteins; 2.1 Introduction; 2.2 Stability of β-Barrel Membrane Proteins; 2.2.1 Thermodynamic Stability of FepA in Detergent Micelles; 2.2.2 Thermodynamic Stability of OmpA in Phospholipids Bilayers; 2.2.3 Thermal Stability of FhuA in Detergent Micelles 2.3 Insertion and Folding of Transmembrane β-Barrel Proteins2.3.1 Insertion and Folding of β-Barrel Membrane Proteins in Micelles; 2.3.2 Oriented Insertion and Folding into Phospholipid Bilayers; 2.3.3 Assemblies of Amphiphiles Induce Structure Formation in β-Barrel Membrane Proteins; 2.3.4 Electrophoresis as a Tool to Monitor Insertion and Folding of β-Barrel Membrane Proteins; 2.3.5 pH and Lipid Headgroup Dependence of the Folding of β-Barrel Membrane Proteins; 2.4 Kinetics of Membrane Protein Folding 2.4.1 Rate Law for β-Barrel Membrane Protein Folding and Lipid Acyl Chain Length Dependence2.4.2 Synchronized Kinetics of Secondary and Tertiary Structure Formation of the β-Barrel OmpA; 2.4.3 Interaction of OmpA with the Lipid Bilayer is Faster than the Formation of Folded OmpA; 2.5 Folding Mechanism of the β-Barrel of OmpA into DOPC Bilayers; 2.5.1 Multistep Folding Kinetics and Temperature Dependence of OmpA Folding; 2.5.2 Characterization of Folding Intermediates by Fluorescence Quenching; 2.5.3 The β-Barrel Domain of OmpA Folds and Inserts by a Concerted Mechanism 2.6 Protein-Lipid Interactions at the Interface of β-Barrel Membrane Proteins2.6.1 Stoichiometry of the Lipid-Protein Interface; 2.6.2 Lipid Selectivity of β-Barrel Membrane Proteins; 2.7 Orientation of β-Barrel Membrane Proteins in Lipid Bilayers; 2.7.1 Lipid Dependence of the β-Barrel Orientation Relative to the Membrane; 2.7.2 Inclination of the β-Strands Relative to the β-Barrel Axis in Lipid Bilayers; 2.7.3 Hydrophobic Matching of the β-Barrel and the Lipid Bilayer; 2.8 In vivo Requirements for the Folding of OMPs; 2.8.1 Amino Acid Sequence Constraints for OmpA Folding in vivo 2.8.2 Periplasmic Chaperones |
Record Nr. | UNINA-9910143964103321 |
Weinheim, : Wiley-VCH, c2005 | ||
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Lo trovi qui: Univ. Federico II | ||
|
Protein-lipid interactions [[electronic resource] ] : from membrane domains to cellular networks / / edited by Lukas K. Tamm |
Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2005 |
Descrizione fisica | 1 online resource (472 p.) |
Disciplina | 572.68 |
Altri autori (Persone) | TammLukas K |
Soggetto topico |
Membrane proteins
Lipoproteins Lipids Proteins Protein binding Membrane lipids |
ISBN |
1-280-85408-1
9786610854080 3-527-60676-9 3-527-60699-8 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Protein-Lipid Interactions; Preface; Contents; List of Contributors; Part 1 How Lipids Shape Proteins; 1 Lipid Bilayers, Translocons and the Shaping of Polypeptide Structure; 1.1 Introduction; 1.2 Membrane Proteins: Intrinsic Interactions; 1.2.1 Physical Determinants of Membrane Protein Stability: The Bilayer Milieu; 1.2.2 Physical Determinants of Membrane Protein Stability: Energetics of Peptides in Bilayers; 1.2.3 Physical Determinants of Membrane Protein Stability: Helix-Helix Interactions in Bilayers; 1.3 Membrane Proteins: Formative Interactions
1.3.1 Connecting Translocon-assisted Folding to Physical Hydrophobicity Scales: The Interfacial Connection1.3.2 Connecting Translocon-assisted Folding to Physical Hydrophobicity Scales: Transmembrane Insertion of Helices; 1.4 Perspectives; References; 2 Folding and Stability of Monomeric β-Barrel Membrane Proteins; 2.1 Introduction; 2.2 Stability of β-Barrel Membrane Proteins; 2.2.1 Thermodynamic Stability of FepA in Detergent Micelles; 2.2.2 Thermodynamic Stability of OmpA in Phospholipids Bilayers; 2.2.3 Thermal Stability of FhuA in Detergent Micelles 2.3 Insertion and Folding of Transmembrane β-Barrel Proteins2.3.1 Insertion and Folding of β-Barrel Membrane Proteins in Micelles; 2.3.2 Oriented Insertion and Folding into Phospholipid Bilayers; 2.3.3 Assemblies of Amphiphiles Induce Structure Formation in β-Barrel Membrane Proteins; 2.3.4 Electrophoresis as a Tool to Monitor Insertion and Folding of β-Barrel Membrane Proteins; 2.3.5 pH and Lipid Headgroup Dependence of the Folding of β-Barrel Membrane Proteins; 2.4 Kinetics of Membrane Protein Folding 2.4.1 Rate Law for β-Barrel Membrane Protein Folding and Lipid Acyl Chain Length Dependence2.4.2 Synchronized Kinetics of Secondary and Tertiary Structure Formation of the β-Barrel OmpA; 2.4.3 Interaction of OmpA with the Lipid Bilayer is Faster than the Formation of Folded OmpA; 2.5 Folding Mechanism of the β-Barrel of OmpA into DOPC Bilayers; 2.5.1 Multistep Folding Kinetics and Temperature Dependence of OmpA Folding; 2.5.2 Characterization of Folding Intermediates by Fluorescence Quenching; 2.5.3 The β-Barrel Domain of OmpA Folds and Inserts by a Concerted Mechanism 2.6 Protein-Lipid Interactions at the Interface of β-Barrel Membrane Proteins2.6.1 Stoichiometry of the Lipid-Protein Interface; 2.6.2 Lipid Selectivity of β-Barrel Membrane Proteins; 2.7 Orientation of β-Barrel Membrane Proteins in Lipid Bilayers; 2.7.1 Lipid Dependence of the β-Barrel Orientation Relative to the Membrane; 2.7.2 Inclination of the β-Strands Relative to the β-Barrel Axis in Lipid Bilayers; 2.7.3 Hydrophobic Matching of the β-Barrel and the Lipid Bilayer; 2.8 In vivo Requirements for the Folding of OMPs; 2.8.1 Amino Acid Sequence Constraints for OmpA Folding in vivo 2.8.2 Periplasmic Chaperones |
Record Nr. | UNINA-9910830401503321 |
Weinheim, : Wiley-VCH, c2005 | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
|
Protein-lipid interactions : from membrane domains to cellular networks / / edited by Lukas K. Tamm |
Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2005 |
Descrizione fisica | 1 online resource (472 p.) |
Disciplina | 572/.696 |
Altri autori (Persone) | TammLukas K |
Soggetto topico |
Membrane proteins
Lipoproteins Lipids Proteins Protein binding Membrane lipids |
ISBN |
1-280-85408-1
9786610854080 3-527-60676-9 3-527-60699-8 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Protein-Lipid Interactions; Preface; Contents; List of Contributors; Part 1 How Lipids Shape Proteins; 1 Lipid Bilayers, Translocons and the Shaping of Polypeptide Structure; 1.1 Introduction; 1.2 Membrane Proteins: Intrinsic Interactions; 1.2.1 Physical Determinants of Membrane Protein Stability: The Bilayer Milieu; 1.2.2 Physical Determinants of Membrane Protein Stability: Energetics of Peptides in Bilayers; 1.2.3 Physical Determinants of Membrane Protein Stability: Helix-Helix Interactions in Bilayers; 1.3 Membrane Proteins: Formative Interactions
1.3.1 Connecting Translocon-assisted Folding to Physical Hydrophobicity Scales: The Interfacial Connection1.3.2 Connecting Translocon-assisted Folding to Physical Hydrophobicity Scales: Transmembrane Insertion of Helices; 1.4 Perspectives; References; 2 Folding and Stability of Monomeric β-Barrel Membrane Proteins; 2.1 Introduction; 2.2 Stability of β-Barrel Membrane Proteins; 2.2.1 Thermodynamic Stability of FepA in Detergent Micelles; 2.2.2 Thermodynamic Stability of OmpA in Phospholipids Bilayers; 2.2.3 Thermal Stability of FhuA in Detergent Micelles 2.3 Insertion and Folding of Transmembrane β-Barrel Proteins2.3.1 Insertion and Folding of β-Barrel Membrane Proteins in Micelles; 2.3.2 Oriented Insertion and Folding into Phospholipid Bilayers; 2.3.3 Assemblies of Amphiphiles Induce Structure Formation in β-Barrel Membrane Proteins; 2.3.4 Electrophoresis as a Tool to Monitor Insertion and Folding of β-Barrel Membrane Proteins; 2.3.5 pH and Lipid Headgroup Dependence of the Folding of β-Barrel Membrane Proteins; 2.4 Kinetics of Membrane Protein Folding 2.4.1 Rate Law for β-Barrel Membrane Protein Folding and Lipid Acyl Chain Length Dependence2.4.2 Synchronized Kinetics of Secondary and Tertiary Structure Formation of the β-Barrel OmpA; 2.4.3 Interaction of OmpA with the Lipid Bilayer is Faster than the Formation of Folded OmpA; 2.5 Folding Mechanism of the β-Barrel of OmpA into DOPC Bilayers; 2.5.1 Multistep Folding Kinetics and Temperature Dependence of OmpA Folding; 2.5.2 Characterization of Folding Intermediates by Fluorescence Quenching; 2.5.3 The β-Barrel Domain of OmpA Folds and Inserts by a Concerted Mechanism 2.6 Protein-Lipid Interactions at the Interface of β-Barrel Membrane Proteins2.6.1 Stoichiometry of the Lipid-Protein Interface; 2.6.2 Lipid Selectivity of β-Barrel Membrane Proteins; 2.7 Orientation of β-Barrel Membrane Proteins in Lipid Bilayers; 2.7.1 Lipid Dependence of the β-Barrel Orientation Relative to the Membrane; 2.7.2 Inclination of the β-Strands Relative to the β-Barrel Axis in Lipid Bilayers; 2.7.3 Hydrophobic Matching of the β-Barrel and the Lipid Bilayer; 2.8 In vivo Requirements for the Folding of OMPs; 2.8.1 Amino Acid Sequence Constraints for OmpA Folding in vivo 2.8.2 Periplasmic Chaperones |
Record Nr. | UNINA-9910877394203321 |
Weinheim, : Wiley-VCH, c2005 | ||
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Lo trovi qui: Univ. Federico II | ||
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Rab GTPases and membrane trafficking [[electronic resource] /] / edited by Guangpu Li & Nava Segev |
Pubbl/distr/stampa | [Dubai, United Arab Emirates], : Bentham eBooks, [2012] |
Descrizione fisica | 1 online resource (180 p.) |
Disciplina |
571.6
612/.01575 |
Altri autori (Persone) |
LiGuangpu
SegevNava |
Soggetto topico |
Guanosine triphosphate
GTPase-activating protein Cell membranes Membrane proteins Membrane lipids Biological transport |
Soggetto genere / forma | Electronic books. |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
01 Title.pdf; 02 Cover Page; 03 REVISED eBooks End User License Agreement-Website; 04 CONTENT; 05 Foreword; 06 Preface; 07 Contributors; 08 Chapter 1 Li&SegevOVChpter1-Rev3; 09 Chapter 2 SegevYpt1Chpter2-Rev3; 10 Chapter 3 GoudRab6Chpter3-Rev3; 11 Chapter 4 GuoSec4pChpter4-Rev3; 12 Chapter 5 DarchenRab3Chpter5-Rev3; 13 Chapter 6 HammerRab27Chpter6-Rev3; 14 Chapter 7 LIRab5Chpter7-Rev3; 15 Chapter 8 vanderSluijsRab4Chpter8-Rev3; 16 Chapter 9 GoldenringRab11Chpter9-Rev3; 17 Chapter 10 UngermannRab7Chpter10-Rev3; 18 Chapter 11 PfefferRab9Chapter11-Rev3; 19 Chapter 12 Pereira-LealRabChpter12-Rev3
20 Index |
Record Nr. | UNINA-9910452620103321 |
[Dubai, United Arab Emirates], : Bentham eBooks, [2012] | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
|
Rab GTPases and membrane trafficking [[electronic resource] /] / edited by Guangpu Li & Nava Segev |
Pubbl/distr/stampa | [Dubai, United Arab Emirates], : Bentham eBooks, [2012] |
Descrizione fisica | 1 online resource (180 p.) |
Disciplina |
571.6
612/.01575 |
Altri autori (Persone) |
LiGuangpu
SegevNava |
Soggetto topico |
Guanosine triphosphate
GTPase-activating protein Cell membranes Membrane proteins Membrane lipids Biological transport |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
01 Title.pdf; 02 Cover Page; 03 REVISED eBooks End User License Agreement-Website; 04 CONTENT; 05 Foreword; 06 Preface; 07 Contributors; 08 Chapter 1 Li&SegevOVChpter1-Rev3; 09 Chapter 2 SegevYpt1Chpter2-Rev3; 10 Chapter 3 GoudRab6Chpter3-Rev3; 11 Chapter 4 GuoSec4pChpter4-Rev3; 12 Chapter 5 DarchenRab3Chpter5-Rev3; 13 Chapter 6 HammerRab27Chpter6-Rev3; 14 Chapter 7 LIRab5Chpter7-Rev3; 15 Chapter 8 vanderSluijsRab4Chpter8-Rev3; 16 Chapter 9 GoldenringRab11Chpter9-Rev3; 17 Chapter 10 UngermannRab7Chpter10-Rev3; 18 Chapter 11 PfefferRab9Chapter11-Rev3; 19 Chapter 12 Pereira-LealRabChpter12-Rev3
20 Index |
Record Nr. | UNINA-9910779493703321 |
[Dubai, United Arab Emirates], : Bentham eBooks, [2012] | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
|
Rab GTPases and membrane trafficking [[electronic resource] /] / edited by Guangpu Li & Nava Segev |
Edizione | [1st ed.] |
Pubbl/distr/stampa | [Dubai, United Arab Emirates], : Bentham eBooks, [2012] |
Descrizione fisica | 1 online resource (180 p.) |
Disciplina |
571.6
612/.01575 |
Altri autori (Persone) |
LiGuangpu
SegevNava |
Soggetto topico |
Guanosine triphosphate
GTPase-activating protein Cell membranes Membrane proteins Membrane lipids Biological transport |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
01 Title.pdf; 02 Cover Page; 03 REVISED eBooks End User License Agreement-Website; 04 CONTENT; 05 Foreword; 06 Preface; 07 Contributors; 08 Chapter 1 Li&SegevOVChpter1-Rev3; 09 Chapter 2 SegevYpt1Chpter2-Rev3; 10 Chapter 3 GoudRab6Chpter3-Rev3; 11 Chapter 4 GuoSec4pChpter4-Rev3; 12 Chapter 5 DarchenRab3Chpter5-Rev3; 13 Chapter 6 HammerRab27Chpter6-Rev3; 14 Chapter 7 LIRab5Chpter7-Rev3; 15 Chapter 8 vanderSluijsRab4Chpter8-Rev3; 16 Chapter 9 GoldenringRab11Chpter9-Rev3; 17 Chapter 10 UngermannRab7Chpter10-Rev3; 18 Chapter 11 PfefferRab9Chapter11-Rev3; 19 Chapter 12 Pereira-LealRabChpter12-Rev3
20 Index |
Record Nr. | UNINA-9910823250803321 |
[Dubai, United Arab Emirates], : Bentham eBooks, [2012] | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
|
Transmembrane dynamic lipids [[electronic resource] /] / edited by Philippe Devaux, Andreas Herrmann |
Pubbl/distr/stampa | Hoboken, N.J., : Wiley, 2012 |
Descrizione fisica | 1 online resource (442 p.) |
Disciplina | 572/.577 |
Altri autori (Persone) |
DevauxPhilippe F
HerrmannAndreas |
Collana | The Wiley series in protein and peptide science |
Soggetto topico |
Membrane lipids
Cell membranes Biological transport |
ISBN |
1-283-28116-3
9786613281166 1-118-12010-8 1-118-12011-6 1-118-12008-6 |
Classificazione | SCI007000 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto | pt. 1. Assessing transmembrane movement and asymmetry of lipids -- pt. 2. Lipid asymmetry in cell membranes -- pt. 3. Energy-independent protein-mediated transmembrane movement of lipids -- pt. 4. Energy-dependent lipid transport across membranes -- pt. 5. Relevance of lipid transmembrane distribution for membrane properties and processes -- pt. 6. Apoptosis and diseases : consequences of disruption to lipid transmembrane asymmetry. |
Record Nr. | UNINA-9910139718403321 |
Hoboken, N.J., : Wiley, 2012 | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
|
Transmembrane dynamic lipids / / edited by Philippe Devaux, Andreas Herrmann |
Edizione | [1st ed.] |
Pubbl/distr/stampa | Hoboken, N.J., : Wiley, 2012 |
Descrizione fisica | 1 online resource (442 p.) |
Disciplina | 572/.577 |
Altri autori (Persone) |
DevauxPhilippe F
HerrmannAndreas |
Collana | The Wiley series in protein and peptide science |
Soggetto topico |
Membrane lipids
Cell membranes Biological transport |
ISBN |
1-283-28116-3
9786613281166 1-118-12010-8 1-118-12011-6 1-118-12008-6 |
Classificazione | SCI007000 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto | pt. 1. Assessing transmembrane movement and asymmetry of lipids -- pt. 2. Lipid asymmetry in cell membranes -- pt. 3. Energy-independent protein-mediated transmembrane movement of lipids -- pt. 4. Energy-dependent lipid transport across membranes -- pt. 5. Relevance of lipid transmembrane distribution for membrane properties and processes -- pt. 6. Apoptosis and diseases : consequences of disruption to lipid transmembrane asymmetry. |
Record Nr. | UNINA-9910813233003321 |
Hoboken, N.J., : Wiley, 2012 | ||
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Lo trovi qui: Univ. Federico II | ||
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