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Protein-lipid interactions [[electronic resource] ] : from membrane domains to cellular networks / / edited by Lukas K. Tamm
| 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 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein-lipid interactions [[electronic resource] ] : from membrane domains to cellular networks / / edited by Lukas K. Tamm
| 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 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein-lipid interactions : from membrane domains to cellular networks / / edited by Lukas K. Tamm
| 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 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||