Protein instability during HIC: Evidence of unfolding reversibility, and apparent adsorption strength of disulfide bond-reduced α-lactalbumin variants

Biotechnology and Bioengineering

Volumn 102, Issue 5, 2009, Pages 1416-1427

  Deitcher, R W ^a   Xiao, Y ^a   O'Connell, J P ^a   Fernandez, E J ^a  

^a University of Virginia   (United States)

Author keywords

Hydrophobic interaction chromatography; Lactalbumin; Protein instability

Indexed keywords

APPARENT ADSORPTIONS; CONFORMATIONAL STABILITIES; DEUTERIUM LABELING; DISULFIDE BONDS; FREE ENERGY CHANGES; HYDROPHOBIC INTERACTION CHROMATOGRAPHY; LACTALBUMIN; MELTING TEMPERATURES; MODEL PROTEINS; PROTEIN ADSORPTIONS; PROTEIN INSTABILITY; SALT CONCENTRATIONS; STATE MODELS; STUDY AND APPLICATIONS; SURFACE UNFOLDING; WILD-TYPE PROTEINS;

ADSORPTION; CHROMATOGRAPHIC ANALYSIS; CONFORMATIONS; DEUTERIUM; HYDROPHOBICITY; MELTING POINT; RESINS; STABILITY;

HYDROPHOBIC CHROMATOGRAPHY;

ALPHA LACTALBUMIN; CALCIUM; SODIUM CHLORIDE;

ADSORPTION; ARTICLE; CHROMATOGRAPHY; CONTROLLED STUDY; DEUTERIUM HYDROGEN EXCHANGE; DISULFIDE BOND; KINETICS; MELTING POINT; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN VARIANT; SYNTHESIS;

ADSORPTION; CHROMATOGRAPHY; DEUTERIUM; DISULFIDES; HYDROPHOBICITY; KINETICS; LACTALBUMIN; MODELS, MOLECULAR; OXIDATION-REDUCTION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; STAINING AND LABELING;

EID: 63549149917     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.22171     Document Type: Article

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