Role of the domain-domain interaction in the construction of the antigen combining site. A comparative study by 1H-15N shift correlation NMR spectroscopy of the Fv and Fab fragments of anti-dansyl mouse monoclonal antibody.

Takahashi, H; Tamura, H; Shimba, N; Shimada, I; Arata, Y

Takahashi, H; Tamura, H; Shimba, N; Shimada, I; Arata, Y.

Affiliation

Takahashi H; Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.

J Mol Biol ; 243(3): 494-503, 1994 Oct 28.

Article in En | MEDLINE | ID: mdl-7966275

Subject(s)

Antibodies, Monoclonal/chemistry; Binding Sites, Antibody/physiology; Immunoglobulin Fab Fragments/chemistry; Immunoglobulin Variable Region/chemistry; Protein Conformation; Amides/chemistry; Animals; Dansyl Compounds/metabolism; Immunoglobulin Fab Fragments/metabolism; Immunoglobulin Variable Region/metabolism; Magnetic Resonance Spectroscopy; Mice; Molecular Structure; Protein Binding; Protons; Thermodynamics

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Database: MEDLINE Main subject: Protein Conformation / Binding Sites, Antibody / Immunoglobulin Variable Region / Immunoglobulin Fab Fragments / Antibodies, Monoclonal Limits: Animals Language: En Journal: J Mol Biol Year: 1994 Type: Article Affiliation country: Japan

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