Oxidative Folding of Proteins

1. Principles and Analysis of Disulphide Bond Formation: 1.1 Disulphide bonds in protein folding and stability, 1.2 Techniques to monitor disulphide-bond formation and the reduction potential of cysteine-cystine couples in vitro and in vivo, 1.3 Real Time Detection of Thiol Chemistry in Single Proteins, 1.4 Analysis of disulphide bond formation in therapeutic proteins. 2. Disulphide Bonds In Peptides And Proteins: Structure, Function And Evolution: 2.1 Evolutionary adaptations to cystine-rich peptide folding, 2.2 In vitro refolding of proteins, 2.3 Allosteric disulphide bonds. 3. Oxidative Folding In The Cell: 3.1 Disulphide bond formation and isomierzation in Escherichia coli, 3.2 Disulphide bond formation in mitochondria, 3.3 Structural insights into disulphide bond formation and protein quality control in the mammalian endoplasmic reticulum, 2.4 Mechanisms of Oxidative Protein Folding and Thiol-Dependent Quality Control: Tales of Cysteines and Cystines, 2.5 Disulphide Bond Formation Downstream of the Endoplasmic Reticulum. 4. Oxidative Folding And Cellular/Organism Homeostasis: 4.1 How microbes cope with oxidative stress, 4.2 Disulphide Bond Formation in the Endoplasmic Reticulum, 4.3 Redox Regulation of Hsp70 Chaperone Function in the Endoplasmic Reticulum, 4.4 Thioredoxin and cellular redox systems: beyond protein disulfide bond reduction. 5. Engineering Covalent Linkages In Peptides And Proteins: 5.1 Stabilization of Peptides and Proteins by Engineered Disulphide Bonds, 5.2 Using genetic code expansion for covalent linkages in proteins