Determination of membrane protein stability via thermodynamic coupling of folding to thiol-disulfide interchange

Protein Science

Volumn 12, Issue 8, 2003, Pages 1732-1740

  Cristian, Lidia ^a   Lear, James D ^a   Degrado, William F ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Folding; Membrane proteins; Thermodynamics; Thiol disulfide interchange

Indexed keywords

AMANTADINE; DISULFIDE; DISULFIDE DECYLPHOSPHOCHOLINE; GLUTATHIONE; MEMBRANE PROTEIN; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

ALPHA HELIX; ANALYTIC METHOD; ARTICLE; BILAYER MEMBRANE; CHEMISTRY; CROSS LINKING; DRUG DETERMINATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; INFLUENZA VIRUS A; KINETICS; METABOLISM; MICELLE; NONHUMAN; OLIGOMERIZATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; PROTEIN STABILITY; THERMODYNAMICS; ULTRACENTRIFUGATION;

CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DISULFIDES; GLUTATHIONE; KINETICS; MEMBRANE PROTEINS; MICELLES; OXIDATION-REDUCTION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; SULFHYDRYL COMPOUNDS; THERMODYNAMICS; ULTRACENTRIFUGATION;

INFLUENZA A VIRUS; INFLUENZA VIRUS;

EID: 0041914460     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0378603     Document Type: Article

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