000 04170nam a22005175i 4500
001 978-1-4419-7273-6
003 DE-He213
005 20140220083723.0
007 cr nn 008mamaa
008 110811s2011 xxu| s |||| 0|eng d
020 _a9781441972736
_9978-1-4419-7273-6
024 7 _a10.1007/978-1-4419-7273-6
_2doi
050 4 _aQH345
050 4 _aQD415-436
072 7 _aPSB
_2bicssc
072 7 _aSCI007000
_2bisacsh
082 0 4 _a572
_223
100 1 _aChang, Rowen J. Y.
_eeditor.
245 1 0 _aFolding of Disulfide Proteins
_h[electronic resource] /
_cedited by Rowen J. Y. Chang, Salvador Ventura.
264 1 _aNew York, NY :
_bSpringer New York,
_c2011.
300 _aX, 286 p.
_bonline resource.
336 _atext
_btxt
_2rdacontent
337 _acomputer
_bc
_2rdamedia
338 _aonline resource
_bcr
_2rdacarrier
347 _atext file
_bPDF
_2rda
490 1 _aProtein Reviews ;
_v14
505 0 _aOxidative 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.
520 _aDisulfide-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.
650 0 _aLife sciences.
650 0 _aBiochemistry.
650 0 _aCytology.
650 1 4 _aLife Sciences.
650 2 4 _aBiochemistry, general.
650 2 4 _aAnimal Biochemistry.
650 2 4 _aMedical Biochemistry.
650 2 4 _aCell Biology.
650 2 4 _aBiophysics and Biological Physics.
700 1 _aVentura, Salvador.
_eeditor.
710 2 _aSpringerLink (Online service)
773 0 _tSpringer eBooks
776 0 8 _iPrinted edition:
_z9781441972729
830 0 _aProtein Reviews ;
_v14
856 4 0 _uhttp://dx.doi.org/10.1007/978-1-4419-7273-6
912 _aZDB-2-SBL
999 _c105726
_d105726