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Protein aggregation in bacteria : functional and structural properties of inclusion bodies in bacterial cells / / edited by Silvia Maria Doglia, Marina Lotti
| Protein aggregation in bacteria : functional and structural properties of inclusion bodies in bacterial cells / / edited by Silvia Maria Doglia, Marina Lotti |
| Pubbl/distr/stampa | Hoboken, New Jersey : , : Wiley, , 2014 |
| Descrizione fisica | 1 online resource (300 p.) |
| Disciplina | 572/.69 |
| Collana | Wiley Series in Protein and Peptide Science |
| Soggetto topico | Bacterial proteins |
| ISBN |
1-118-84536-6
1-118-85503-5 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Protein Aggregation in Bacteria: Functional and Structural Properties of Inclusion Bodies in Bacterial Cells; Copyright; Contents; Contributors; Preface ; Introduction to the WileySeries in Protein and PeptideScience; 1 Fundamentals of Protein Folding ; 1.1 Folding-misfolding-nonfolding crossroads; 1.2 Protein folding; 1.2.1 Protein-Folding Code; 1.2.2 Protein-Folding Models; 1.2.3 Polymer Aspects of Protein Folding; 1.2.4 Different Conformations Seen in Protein Folding; 1.3 Nonfolding; 1.3.1 Intrinsically Disordered Proteins and Their Abundance; 1.3.2 Some Functional Advantages of IDPs
1.3.3 Function-Induced Folding of IDPs1.3.4 IDPs and Human Diseases; 1.3.5 How Does an Amino Acid Sequence Encode Intrinsic Disorder?; 1.3.6 Polymer Aspects of Nonfolding; 1.4 Misfolding; 1.4.1 Molecular Mechanisms of Protein Misfolding; 1.4.2 Fibrillogenesis of Globular Proteins: Requirement for Partial Unfolding; 1.4.3 Fibrillogenesis of IDPs: Requirement for Partial Folding; 1.4.4 Conformational Prerequisites for Amyloidogenesis; 1.4.5 Multiple Pathways of Protein Misfolding; 1.4.6 Polymer Aspects of Protein Misfolding; References 2 Recruiting Unfolding Chaperones to Solubilize Misfolded Recombinant Proteins 2.1 Introduction; 2.2 Chemical Chaperones; 2.3 PPIs and PDIs are folding enzymes; 2.4 Molecular Chaperones; 2.5 The small Hsps; 2.6 Hsp90 ; 2.7 Hsp70/Hsp40; 2.8 GroEL Chaperonins; 2.9 Conclusions; References; 3 Osmolytes as Chemical Chaperones to Use in Protein Biotechnology ; 3.1 Introduction; 3.2 Protein-destabilizing conditions and counteracting mechanisms: shared or independent routes?; 3.3 Proposed molecular mechanisms for osmolyte activities; 3.4 Osmolytes and expression of recombinant proteins 3.5 Biotechnological relevance of osmolytes for preserving purified proteins3.6 Conclusions; References; 4 Inclusion Bodies in the Study of Amyloid Aggregation ; 4.1 Introduction; 4.2 Structure of IBs ; 4.2.1 Amyloid-like Nature of IBs ; 4.2.2 Detection and Characterization of Amyloid Conformations Inside IBs ; 4.3 Formation of IBs ; 4.3.1 In Vivo Formation Kinetics; 4.3.2 Molecular Determinants of IB Aggregation; 4.3.3 Sequence Specificity in IB Formation; 4.4 IBs as the simplest model for in vivo amyloid toxicity; 4.4.1 The Fitness Cost of Amyloid Aggregation 4.4.2 Citotoxicity of Amyloid IBs 4.4.3 Infectious Properties of IBs ; 4.5 Using IBs to screen for amyloid inhibitors; 4.6 Conclusions; References; 5 Protein Aggregation in Unicellular Eukaryotes ; 5.1 Introduction; 5.2 UPR: Unfolded protein response in the ER; 5.3 Removing persistent misfolded proteins with the proteasome; 5.4 Lysosomal/vacuolar proteolysis (overload UPS); 5.4.1 Autophagy; 5.4.2 Selective Types of Autophagy; 5.5 Refolding of protein aggregates in cytosol and nucleus; 5.6 JUNQ and IPOD; 5.7 Segregation of aggregates in yeast 5.8 Proteins forming nonpathological amyloid-like fibrils in unicellular eukaryotes |
| Record Nr. | UNINA-9910139119803321 |
| Hoboken, New Jersey : , : Wiley, , 2014 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein aggregation in bacteria : functional and structural properties of inclusion bodies in bacterial cells / / edited by Silvia Maria Doglia, Marina Lotti
| Protein aggregation in bacteria : functional and structural properties of inclusion bodies in bacterial cells / / edited by Silvia Maria Doglia, Marina Lotti |
| Pubbl/distr/stampa | Hoboken, New Jersey : , : Wiley, , 2014 |
| Descrizione fisica | 1 online resource (300 p.) |
| Disciplina | 572/.69 |
| Collana | Wiley Series in Protein and Peptide Science |
| Soggetto topico | Bacterial proteins |
| ISBN |
1-118-84536-6
1-118-85503-5 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Protein Aggregation in Bacteria: Functional and Structural Properties of Inclusion Bodies in Bacterial Cells; Copyright; Contents; Contributors; Preface ; Introduction to the WileySeries in Protein and PeptideScience; 1 Fundamentals of Protein Folding ; 1.1 Folding-misfolding-nonfolding crossroads; 1.2 Protein folding; 1.2.1 Protein-Folding Code; 1.2.2 Protein-Folding Models; 1.2.3 Polymer Aspects of Protein Folding; 1.2.4 Different Conformations Seen in Protein Folding; 1.3 Nonfolding; 1.3.1 Intrinsically Disordered Proteins and Their Abundance; 1.3.2 Some Functional Advantages of IDPs
1.3.3 Function-Induced Folding of IDPs1.3.4 IDPs and Human Diseases; 1.3.5 How Does an Amino Acid Sequence Encode Intrinsic Disorder?; 1.3.6 Polymer Aspects of Nonfolding; 1.4 Misfolding; 1.4.1 Molecular Mechanisms of Protein Misfolding; 1.4.2 Fibrillogenesis of Globular Proteins: Requirement for Partial Unfolding; 1.4.3 Fibrillogenesis of IDPs: Requirement for Partial Folding; 1.4.4 Conformational Prerequisites for Amyloidogenesis; 1.4.5 Multiple Pathways of Protein Misfolding; 1.4.6 Polymer Aspects of Protein Misfolding; References 2 Recruiting Unfolding Chaperones to Solubilize Misfolded Recombinant Proteins 2.1 Introduction; 2.2 Chemical Chaperones; 2.3 PPIs and PDIs are folding enzymes; 2.4 Molecular Chaperones; 2.5 The small Hsps; 2.6 Hsp90 ; 2.7 Hsp70/Hsp40; 2.8 GroEL Chaperonins; 2.9 Conclusions; References; 3 Osmolytes as Chemical Chaperones to Use in Protein Biotechnology ; 3.1 Introduction; 3.2 Protein-destabilizing conditions and counteracting mechanisms: shared or independent routes?; 3.3 Proposed molecular mechanisms for osmolyte activities; 3.4 Osmolytes and expression of recombinant proteins 3.5 Biotechnological relevance of osmolytes for preserving purified proteins3.6 Conclusions; References; 4 Inclusion Bodies in the Study of Amyloid Aggregation ; 4.1 Introduction; 4.2 Structure of IBs ; 4.2.1 Amyloid-like Nature of IBs ; 4.2.2 Detection and Characterization of Amyloid Conformations Inside IBs ; 4.3 Formation of IBs ; 4.3.1 In Vivo Formation Kinetics; 4.3.2 Molecular Determinants of IB Aggregation; 4.3.3 Sequence Specificity in IB Formation; 4.4 IBs as the simplest model for in vivo amyloid toxicity; 4.4.1 The Fitness Cost of Amyloid Aggregation 4.4.2 Citotoxicity of Amyloid IBs 4.4.3 Infectious Properties of IBs ; 4.5 Using IBs to screen for amyloid inhibitors; 4.6 Conclusions; References; 5 Protein Aggregation in Unicellular Eukaryotes ; 5.1 Introduction; 5.2 UPR: Unfolded protein response in the ER; 5.3 Removing persistent misfolded proteins with the proteasome; 5.4 Lysosomal/vacuolar proteolysis (overload UPS); 5.4.1 Autophagy; 5.4.2 Selective Types of Autophagy; 5.5 Refolding of protein aggregates in cytosol and nucleus; 5.6 JUNQ and IPOD; 5.7 Segregation of aggregates in yeast 5.8 Proteins forming nonpathological amyloid-like fibrils in unicellular eukaryotes |
| Record Nr. | UNINA-9910813330403321 |
| Hoboken, New Jersey : , : Wiley, , 2014 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||