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.
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