Biophysical properties of camelid VHH domains compared to those of human VH3 domains

Biochemistry

Volumn 41, Issue 11, 2002, Pages 3628-3636

  Ewert, Stefan ^a   Cambillau, Christian ^b   Conrath, Katja ^c   Plückthun, Andreas ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

^b CNRS   (France)

^c DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ACTIVITY;

ANTIBODIES; FREE ENERGY; HUMAN ENGINEERING;

BIOCHEMISTRY;

IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN;

ARTICLE; ARTIODACTYLA; BINDING AFFINITY; BIOPHYSICS; CONTROLLED STUDY; HUMAN; HYDROPHOBICITY; MELTING POINT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; SPECIES DIFFERENCE; TEMPERATURE DEPENDENCE;

AMINO ACID SEQUENCE; ANIMALS; BIOPHYSICS; CAMELS; CHROMATOGRAPHY, GEL; HUMANS; IMMUNOGLOBULIN HEAVY CHAINS; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN DENATURATION; SEQUENCE HOMOLOGY, AMINO ACID;

ARTIODACTYLA; CAMELIDAE; MURINAE;

EID: 0037133506     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi011239a     Document Type: Article

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