LEADER 05226nam 2200589 450 001 9910139119803321 005 20230803221257.0 010 $a1-118-84536-6 010 $a1-118-85503-5 035 $a(CKB)2550000001273730 035 $a(EBL)1666525 035 $a(OCoLC)867001331 035 $a(MiAaPQ)EBC1666525 035 $a(Au-PeEL)EBL1666525 035 $a(CaPaEBR)ebr10861013 035 $a(CaONFJC)MIL595761 035 $a(EXLCZ)992550000001273730 100 $a20140504h20142014 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $2rdacontent 182 $2rdamedia 183 $2rdacarrier 200 00$aProtein aggregation in bacteria $efunctional and structural properties of inclusion bodies in bacterial cells /$fedited by Silvia Maria Doglia, Marina Lotti 210 1$aHoboken, New Jersey :$cWiley,$d2014. 210 4$dİ2014 215 $a1 online resource (300 p.) 225 1 $aWiley Series in Protein and Peptide Science 300 $aDescription based upon print version of record. 311 $a1-118-44852-9 311 $a1-306-64510-7 320 $aIncludes bibliographical references at the end of each chapters and index. 327 $aProtein 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 327 $a1.3.3 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 327 $a2 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 327 $a3.5 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 327 $a4.4.2 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 327 $a5.8 Proteins forming nonpathological amyloid-like fibrils in unicellular eukaryotes 330 $aThis book focuses on the aggregation of recombinant proteins in bacterial cells in the form of inclusion bodies. Recent reports revolutionized the current view of inclusion bodies from that of inert deposits of inactive proteins to reservoirs of proteins that can eventually maintain biological activity and/or be rescued by cells. Aggregation is put in the context of updated knowledge about the folding and aggregation of proteins in simple cells and new perspectives derived from the application of this knowledge are presented. The following topics are addressed: a) molecular and c 410 0$aWiley series in protein and peptide science. 606 $aBacterial proteins 615 0$aBacterial proteins. 676 $a572/.69 702 $aDoglia$b Silvia Maria 702 $aLotti$b Marina 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910139119803321 996 $aProtein aggregation in bacteria$91970267 997 $aUNINA