By George Georgiou and Eliana De Bernardez-Clark (Eds.)
content material: Inclusion our bodies and restoration of proteins from the aggregated country / Eliana De Barnardez-Clark and George Georgiou --
actual equipment and types for the learn of protein aggregation / Catherine H. Schein --
Mechanisms of inclusion physique formation / Anna Mitraki, Cameron Haase-Pettingell, and Jonathan King --
constitution and balance of cytochrome c folding intermediates / Gülnur A. Elöve and Heinrich Roder --
Thermostability of drifted oligomeric, diminished, and refolded proteins / S.L. Sagar and M.M. Domach --
Oxidative refolding of recombinant human glia maturation issue beta / Asgar Zaheer and Ramon Lim --
restricted proteolysis of solvent-induced folding alterations of [beta]-lactoglobulin / M. Dalgalarrondo ... [et al.] --
Folding and aggregation of RTEM [beta]-lactamase / Pascal Valax and George Georgiou --
position of chaperonins in protein folding / Pierre Goloubinoff, Anthony A. Gatenby, and George H. Lorimer --
Pathway for the thermal unfolding of untamed sort and mutant varieties of the thermostable P22 tailspike endorhamnosidase / Bao-lu Chen and Jonathan King --
Kinetics of inclusion physique formation in Escherichia coli CY15070 generating prochymosin / Alfred Carlson and Jayanthi Reddy --
lively creatine kinase refolded from inclusion our bodies in Escherichia coli : better restoration by way of elimination of contaminating protease / Patricia C. Babbitt ... [et al.] --
Equilibrium organization of a molten globule intermediate within the refolding of bovine carbonic anhydrase / Jeffrey L. Cleland and Daniel I.C. Wang --
An engineering method of reaching high-protein refolding yields / Steven Vicik and Eliana De Bernardez-Clark --
Commercial-scale refolding of recombinant methionyl bovine somatotropin / S. Bradley Storrs and Todd M. Przybycien --
Large-scale refolding of secretory leukocyte protease inhibitor / Robert J. Seely and Mark D. Young.
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Additional resources for Protein Refolding
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The crystals were frozen at various stages of growth ( the growth rate of the crystals was regulated by varying the concentration of protein in the mother liquid) in liquid xenon and platinum-carbon replicas were prepared of the growing crystal surface. Nucleation sites were then calculated (using a simple model)fromthe superposition pattern of the monomolecular-layers observed. The nucleation sites per crystal so estimated were exponentially related to the lysozyme concentration in the mother liquor.