Folding of Disulfide Proteins

Herausgegeben:Chang, Rowen J.-Y.; Ventura, Salvador

• Gebundenes Buch

Produktbeschreibung

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.

Produktdetails

• Protein Reviews 14
• Verlag: Springer / Springer New York / Springer, Berlin
• Artikelnr. des Verlages: 12641314, 978-1-4419-7272-9
• 2011
• Seitenzahl: 296
• Erscheinungstermin: 12. August 2011
• Englisch
• Abmessung: 241mm x 160mm x 20mm
• Gewicht: 555g
• ISBN-13: 9781441972729
• ISBN-10: 1441972722
• Artikelnr.: 30681072

Inhaltsangabe

Oxidative folding: coupling conformational folding and disulfide formation.- The case of oxidative folding of ribonuclease A: Factors impacting fold maturation of ER-processed proteins.- Cystine knot folding in cyclotides.- In vitro folding of single chain/double chain insulin and related protein.- Unfolding and refolding of disulfide proteins via disulfide scrambling.- Small catalysts for Protein oxidative folding.- Protein Disulfide Isomerase and the Catalysis of Oxidative Protein Folding.- Allosteric disulfide bonds.- The problem of expression of multi-disulfide bonded recombinant protein in E. coli.- NMR-spectroscopic investigation of disulfide dynamics in unfolded states of proteins.- A half-century of oxidative folding and protein disulfide formation.