High hydrostatic pressure (HHP) modulates protein–protein and protein–solvent interactions through volume changes and thereby affects the equilibrium of protein conformational species between native and denatured forms as well as monomeric, oligomeric, and aggregated forms without the addition of chemicals or use of high temperature.
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Get PriceWe hypothesize that if the pressure effects on aggregates of nonnative protein molecules are similar to those on native multimeric proteins, then there must exist a “pressure window” where pressure is high enough to solubilize aggregates, but still allow refolding to the native conformation.
Get PriceUnder each of the conditions used to effect complete refolding of rhGH from aggregates by high hydrostatic pressure ( m GdnHCl at 25 °C, or in the absence of GdnHCl at 60 °C), the native state of the protein is highly favored thermodynamically, by ∼25 kJ/mol.
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Get PriceNov 09, 1999· We hypothesize that if the pressure effects on aggregates of nonnative protein molecules are similar to those on native multimeric proteins, then there must exist a “pressure window” where pressure is high enough to solubilize aggregates, but still …
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Get PriceRequest PDF on ResearchGate | High pressure deformation in twophase aggregates | We investigate the rheological behavior of multiphase aggregates at high pressure and high …
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Get PriceInvestigation of the effects of pressure, temperature, and chaotrope on unfolding of rhGH documented that under conditions used for optimal high pressure disaggregation and refolding, the native state is greatly favored thermodynamically ( 25 kJ/mol at 2000 bar and m GdnHCl). Dissolution of aggregates under pressure is a kinetically ...
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Get PriceJin et al. and Zhang et al. performed deformation experiments at a pressure of 3 GPa on aggregates synthesized from natural omphacite crystals with compositions of di 73 jd 27 (73 mol % di; 27 mol % jd) and di 58 jd 42, respectively. Synthetic aggregates of jadeite were examined by Orzol et al. .
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Get PriceHigh pressure fosters protein refolding from aggregates at high concentrations Richard J. St. John*, John F. Carpenter†, and Theodore W. Randolph*‡ *Department of Chemical Engineering, University of Colorado, Boulder, CO 80309; and †Department of Pharmaceutical Science, University of Colorado Health Sciences Center, Denver, CO 80262
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