Refolding of proteins from inclusion bodies is favored by a diminished hydrophobic effect at elevated pressures

Biotechnology and Bioengineering

Volumn 102, Issue 2, 2009, Pages 483-492

  Crisman, Ryan L ^a   Randolph, Theodore W ^a  

^a University of Colorado at Boulder   (United States)

Author keywords

Colloidal stability; Protein folding; Refractive index increment; Second virial coefficient

Indexed keywords

COLLOIDAL STABILITY; DRIVING FORCES; EFFECTIVE TOOLS; ELEVATED PRESSURES; EXPERIMENTAL VALUES; FUNCTION OF PRESSURES; GUANIDINIUM HYDROCHLORIDES; HIGH HYDROSTATIC PRESSURES; HIGH PRESSURES; HYDROPHOBIC EFFECTS; HYDROPHOBIC SURFACES; INCLUSION BODIES; PROTEIN REFOLDING; PROTEIN-PROTEIN INTERACTIONS; RE AGGREGATIONS; REFOLDING; REFRACTIVE INDEX INCREMENT; SECOND VIRIAL COEFFICIENT; T4 LYSOZYMES; UNFOLDED PROTEINS;

ATMOSPHERIC PRESSURE; DISSOLUTION; EQUATIONS OF STATE; HYDROPHOBICITY; HYDROSTATIC PRESSURE; LIGHT REFRACTION; ORGANIC POLYMERS; REFRACTIVE INDEX; REFRACTOMETERS; SURFACE CHEMISTRY;

PROTEIN FOLDING;

GUANIDINE; LYSOZYME; RECOMBINANT PROTEIN;

ARTICLE; ATMOSPHERIC PRESSURE; CELL INCLUSION; CONTROLLED STUDY; ESCHERICHIA COLI; HYDROPHOBICITY; HYDROSTATIC PRESSURE; NONHUMAN; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; REFRACTION INDEX; BACTERIOPHAGE T4; BIOSYNTHESIS; BIOTECHNOLOGY; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; PROTEIN SYNTHESIS; THERMODYNAMICS;

BACTERIOPHAGE T4; BIOTECHNOLOGY; ENZYME STABILITY; ESCHERICHIA COLI; GUANIDINE; HYDROPHOBICITY; HYDROSTATIC PRESSURE; INCLUSION BODIES; MURAMIDASE; PROTEIN BIOSYNTHESIS; PROTEIN CONFORMATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; THERMODYNAMICS;

EID: 58249091623     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.22082     Document Type: Article

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