Studies on the binding sites of IgG2 monoclonal antibodies recognized by terpyridine-based affinity ligands.

Lin, Chih-Pei; Boysen, Reinhard I; Campi, Eva M; Saito, Kei; Hearn, Milton T W

Lin, Chih-Pei; Boysen, Reinhard I; Campi, Eva M; Saito, Kei; Hearn, Milton T W.

Affiliation

Lin CP; School of Chemistry, Monash University, Melbourne, VIC, 3800, Australia.
Boysen RI; School of Chemistry, Monash University, Melbourne, VIC, 3800, Australia.
Campi EM; School of Chemistry, Monash University, Melbourne, VIC, 3800, Australia.
Saito K; School of Chemistry, Monash University, Melbourne, VIC, 3800, Australia.
Hearn MT; School of Chemistry, Monash University, Melbourne, VIC, 3800, Australia.

J Mol Recognit ; 29(7): 334-42, 2016 07.

Article in En | MEDLINE | ID: mdl-26842829

Subject(s)

Antibodies, Monoclonal/chemistry; Antibodies, Monoclonal/metabolism; Immunoglobulin G/chemistry; Immunoglobulin G/metabolism; Amino Acid Motifs; Binding Sites; Calorimetry; Ligands; Models, Molecular; Molecular Docking Simulation; Protein Binding; Thermodynamics

Key words

enthalpic and entropic effects; free energy changes; isothermal titration calorimetry; mixed mode adsorbents; molecular docking; monoclonal antibodies; protein-ligand interactions; terpyridinyl ligands

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Immunoglobulin G / Antibodies, Monoclonal Language: En Journal: J Mol Recognit Journal subject: BIOLOGIA MOLECULAR Year: 2016 Document type: Article Affiliation country: Australia Country of publication: United kingdom

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