Optimization of the antibody CH3 domain by residue frequency analysis of IgG sequences

Journal of Molecular Biology

Volumn 335, Issue 1, 2004, Pages 41-48

  Demarest, Stephen J ^a,b   Rogers, Jeff ^a,b   Hansen, Geneviève ^a,b  

^a SYNGENTA BIOTECHNOLOGY INC   (United States)

^b DIVERSA CORPORATION   (United States)

Author keywords

Antibody; CH3; Immunoglobulin; Protein design; Protein folding

Indexed keywords

ANTIBODY; IMMUNOGLOBULIN G; RECOMBINANT ANTIBODY; THIOREDOXIN REDUCTASE;

AMINO ACID SEQUENCE; ANTIBODY STRUCTURE; ARTICLE; BACTERIAL CELL; BACTERIAL STRAIN; CIRCULAR DICHROISM; COMPARATIVE STUDY; CYTOPLASM; DATA ANALYSIS; EXPERIMENT; FLUORESCENCE; FREQUENCY ANALYSIS; HALF LIFE TIME; MAMMAL; MOLECULAR CLONING; MOLECULE; MUTANT; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STABILITY; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; TEMPERATURE; THERMOSTABILITY;

BACTERIA (MICROORGANISMS); BOVINAE; MAMMALIA; MURINAE;

EID: 0344255687     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.10.040     Document Type: Article

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