Hydrophobic interactions are the driving force for the binding of peptide mimotopes and Staphylococcal protein A to recombinant human IgG1

European Biophysics Journal

Volumn 36, Issue 6, 2007, Pages 647-660

  Arouri, Ahmad ^a   Garidel, Patrick ^b   Kliche, Werner ^b   Blume, Alfred ^a  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

^b BOEHRINGER INGELHEIM PHARMA GMBH AND CO KG   (Germany)

Author keywords

Antibodies; Antigen binding; Isothermal titration calorimetry; Peptide mimotopes; Staphylococcal protein A

Indexed keywords

IMMUNOGLOBULIN G1 ANTIBODY; NANOPARTICLE; RECOMBINANT PROTEIN; SODIUM CHLORIDE; STAPHYLOCOCCUS PROTEIN A;

AMINO ACID SEQUENCE; ANTIGEN BINDING; ARTICLE; BINDING SITE; CONCENTRATION (PARAMETERS); ENTHALPY; ENTROPY; HYDROPHOBICITY; ISOTHERMAL TITRATION CALORIMETRY; MOLECULAR INTERACTION; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; TEMPERATURE; THERMODYNAMICS;

AMINO ACIDS; CALORIMETRY, DIFFERENTIAL SCANNING; HUMANS; HYDROPHOBICITY; IMMUNOGLOBULIN G; PEPTIDES; RECOMBINANT PROTEINS; STAPHYLOCOCCAL PROTEIN A;

EID: 34347384457     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-007-0140-8     Document Type: Article

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