Overview

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.

Full Product Details

Author:   Rowen J. Y. Chang ,  Salvador Ventura
Publisher:   Springer-Verlag New York Inc.
Imprint:   Springer-Verlag New York Inc.
Edition:   2011 ed.
Volume:   14
Dimensions:   Width: 15.50cm , Height: 1.60cm , Length: 23.50cm
Weight:   0.456kg
ISBN:  

9781461429975

ISBN 10:   1461429978
Pages:   286
Publication Date:   24 October 2013
Audience:   College/higher education ,  Postgraduate, Research & Scholarly
Format:   Paperback
Publisher's Status:   Active
Availability:   Manufactured on demand  
We will order this item for you from a manufactured on demand supplier.

Table of Contents

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.

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