Folding of Disulfide Proteins

ISBN-13: 9781461429975 / Angielski / Miękka / 2013 / 286 str.

Rowen J. y. Chang; Salvador Ventura

Opis

This book aims to cover the knowledge of protein folding accumulated from studies of disulfide-containing proteins, including methodologies, folding pathways, and folding mechanism of numerous extensively characterized disulfide proteins. Folding of Disulfide Proteins will be valuable supplementary reading for general biochemistry, biophysics, molecular biology, and cellular biology courses for graduate and undergraduate students. This book can also be used for specialized graduate-level biochemistry, biophysics, and molecular biology courses dedicated to protein folding as well as related biological problems and diseases.Will also be of interest to everybody interested in problems related to protein folding, and anyone who is interested in understanding the mechanism of protein misfolding and protein misfolding-related diseases.

Spis treści

1. Oxidative folding: coupling conformational folding and disulfide formation

Salvador Ventura and  Jui-Yoa Chang

 

2. The case of oxidative folding of ribonuclease A: Factors impacting fold maturation of ER-processed proteins

Mahesh Narayan

 

3. Cystine knot folding in cyclotides

David J. Craik

 

4. In vitro folding of single chain/double chain insulin and related protein

You-Min Feng

 

5. Unfolding and refolding of disulfide proteins via disulfide scrambling

Jui-Yoa Chang

 

6. Small catalysts for Protein oxidative folding        

Watson J. Lees

 

7. Protein Disulfide Isomerase and the Catalysis of Oxidative Protein Folding

Hiram F.  Gilbert

 

8. Allosteric disulfide bonds

Philip J. Hogg

 

9. The problem of expression of multi-disulfide bonded recombinant protein in E. coli

George Georgiou

 

10. NMR-spectroscopic investigation of disulfide dynamics in unfolded states of proteins

Harald Schwalbe

 

11. A half-century of oxidative folding and protein disulfide formation

Robert Freedman

Blurb

Disulfide-containing proteins belong to a unique class of proteins for studying the mechanism of protein folding. Their folding mechanism can be analyzed by three distinct techniques: (1) The conventional denaturation-renaturation method (disulfide intact); (2) The disulfide oxidation method (oxidative folding); and (3) The emerging disulfide scrambling method. Each technique provides specific information as to how an unfolded disulfide protein refolds to form the native structure. This book is intended to highlight the knowledge of several important proteins (BPTI, RNase A, beta-Lactalbumin and Lysozyme etc.) that have been characterized in depth by these methodologies. The book will also devote sections to comparing these methodologies and chaperones (PDI and Dsb machineries) that facilitate folding of disulfide proteins.

Folding of Disulfide Proteins aims to cover the knowledge of protein folding accumulated from studies of disulfide-containing proteins, including methodologies, folding pathways, and folding mechanism of numerous extensively characterized disulfide proteins. This book will be of interest to those interested in problems related to protein folding, and anyone who is interested in understanding the mechanism of protein misfolding and protein misfolding-related diseases.

Folding of Disulfide Proteins aims to cover the knowledge of protein folding accumulated from studies of disulfide-containing proteins, including methodologies, folding pathways, and folding mechanism of numerous extensively characterized disulfide proteins. This book will be of interest to those interested in problems related to protein folding, and anyone who is interested in understanding the mechanism of protein misfolding and protein misfolding-related diseases.