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Volumn 1217, Issue 35, 2010, Pages 5571-5583

Changes in solvent exposure reveal the kinetics and equilibria of adsorbed protein unfolding in hydrophobic interaction chromatography

Author keywords

Hydrophobic interaction chromatography; Kinetics; Protein adsorption; Protein folding; Thermodynamics

Indexed keywords

BULK PHASE; BULK SOLUTIONS; CHROMATOGRAPHIC METHODS; CHROMATOGRAPHIC TECHNIQUES; CONFORMATIONAL STABILITIES; CONFORMATIONAL STATE; DEUTERIUM LABELING; EQUILIBRIUM PARTITIONING; EXPERIMENTAL PROTOCOLS; HYDROGEN EXCHANGE; HYDROPHOBIC INTERACTION CHROMATOGRAPHY; IRREVERSIBLE ADSORPTION; ISOCRATIC; LACTOGLOBULIN; LIGAND CHEMISTRY; MOLECULAR PROPERTIES; PHYSICALLY BASED MODELS; PROTEIN ADSORPTION; PROTEIN RECOVERY; PROTEIN UNFOLDING; PSEUDO FIRST ORDER RATE CONSTANTS; RESIN PROPERTIES; SALT CONCENTRATION; SOLVENT EXPOSURE; SURFACE UNFOLDING; THREE MODELS;

EID: 77955428025     PISSN: 00219673     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chroma.2010.06.051     Document Type: Article
Times cited : (22)

References (62)


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.