Please use this identifier to cite or link to this item: https://doi.org/10.1109/51.582175
Title: Observing interactions between the IgG antigen and anti-IgG antibody with AFM
Authors: Zhang, P.-C.
Bai, C.
Ho, P.K.H. 
Dai, Y.
Wu, Y.-S.
Issue Date: Mar-1997
Citation: Zhang, P.-C., Bai, C., Ho, P.K.H., Dai, Y., Wu, Y.-S. (1997-03). Observing interactions between the IgG antigen and anti-IgG antibody with AFM. IEEE Engineering in Medicine and Biology Magazine 16 (2) : 42-46. ScholarBank@NUS Repository. https://doi.org/10.1109/51.582175
Abstract: Spatially specific interactions between the immonoglobulin G (IgG) antigen and anti-IgG monoclonal antibody (McAb) have been studied in detail by tapping-mode AFM. The binding numbers and binding sites of the antigen molecules with antibody molecules, as well as the conformational changes during the binding process have been revealed. Results showed that: (1) there are spatially specific interactions between IgG and McAb molecules; (2) the binding sites of IgG with McAb molecules are located at four quadrants on the surface of IgG molecules; (3) the binding number of an IgG molecule with McAb may be four; (4) significant morphological changes occurred during reaction of IgG with McAb molecules suggesting that the binding process is accompanied by a conformational change of the proteins involved.
Source Title: IEEE Engineering in Medicine and Biology Magazine
URI: http://scholarbank.nus.edu.sg/handle/10635/107149
ISSN: 07395175
DOI: 10.1109/51.582175
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