X-ray crystallography reveals stringent conservation of protein fold after removal of the only disulfide bridge from a stabilized immunoglobulin variable domain

Folding and Design

Volumn 2, Issue 6, 1997, Pages 357-361

  Usón, Isabel ^a   Teresa Bes, M ^a   Sheldrick, George M ^b   Schneider, Thomas R ^a   Hartsch, Thomas ^a   Fritz, Hans Joachim ^a  

^a UNIVERSITY OF GÖTTINGEN   (Germany)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Antibody engineering; Bence Jones protein; Disulfide free; Protein folding

Indexed keywords

DISULFIDE; IMMUNOGLOBULIN KAPPA CHAIN; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HUMAN; IMMUNOGLOBULIN VARIABLE REGION; METABOLISM; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; DISULFIDES; HUMANS; IMMUNOGLOBULIN KAPPA-CHAINS; IMMUNOGLOBULIN VARIABLE REGION; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS;

EID: 0031302744     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(97)00049-7     Document Type: Article

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