Advanced analyses of kinetic stabilities of iggs modified by mutations and glycosylation

Protein Science

Volumn 24, Issue 7, 2015, Pages 1100-1113

  Sedlák, Erik ^a,b   Schaefer, Jonas V ^a   Marek, Jozef ^c   Gimeson, Peter ^d   Plückthun, Andreas ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

^b P J AFÁRIK UNIVERSITY   (Slovakia)

^c INSTITUTE OF EXPERIMENTAL PHYSICS   (Slovakia)

^d Malvern Instruments Inc   (United States)

Author keywords

differential scanning calorimetry; half life; IgG stability; irreversible transition; kinetic stability; multidomain protein

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN G; IMMUNOGLOBULIN G ANTIBODY; PROTEIN FAB6B3; PROTEIN IGG2C2; PROTEIN IGG6B3; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DEGLYCOSYLATION; DIFFERENTIAL SCANNING CALORIMETRY; HEATING; MATHEMATICAL MODEL; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN GLYCOSYLATION; PROTEIN STABILITY; PROTEIN UNFOLDING; THERMOSTABILITY; TRANSITION TEMPERATURE; ANIMAL; CHEMISTRY; GENETICS; GLYCOSYLATION; HUMAN; KINETICS; MOLECULAR MODEL; MUTATION; PROTEIN TERTIARY STRUCTURE;

ANIMALS; CALORIMETRY, DIFFERENTIAL SCANNING; GLYCOSYLATION; HUMANS; IMMUNOGLOBULIN FAB FRAGMENTS; IMMUNOGLOBULIN G; KINETICS; MODELS, MOLECULAR; MUTATION; PROTEIN DENATURATION; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY;

EID: 84946085093     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2691     Document Type: Article

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