An intrinsically stable antibody scFv fragment can tolerate the loss of both disulfide bonds and fold correctly

FEBS Letters

Volumn 427, Issue 3, 1998, Pages 357-361

  Wörn, Arne ^a   Plückthun, Andreas ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

Antibody engineering; Disulfide bond; Intrabody; Protein stability; ScFv fragment

Indexed keywords

CYSTEINE; DISULFIDE; DITHIOL DERIVATIVE; IMMUNOGLOBULIN FRAGMENT;

ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; ESCHERICHIA COLI; EXPRESSION VECTOR; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; THERMODYNAMICS;

AMINO ACID SUBSTITUTION; BIOSENSING TECHNIQUES; CHROMATOGRAPHY, GEL; CYSTEINE; DISULFIDES; ENZYME-LINKED IMMUNOSORBENT ASSAY; IMMUNOGLOBULIN FRAGMENTS; IMMUNOGLOBULIN HEAVY CHAINS; IMMUNOGLOBULIN LIGHT CHAINS; IMMUNOGLOBULIN VARIABLE REGION; POINT MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; THERMODYNAMICS; UREA;

ESCHERICHIA COLI;

EID: 0032524034     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(98)00463-3     Document Type: Article

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