W e report the predicted combining site structure of the monoclonal antibody fiagmerit, NC10.14, which is specific for the superpotent sweetener, )giranidine acetic acid, using computer-aided molecular modeling and experimental methods, such as fluorescence spectroscopy and circular dichroism. This
Structure of an antibody combining site by magnetic resonance
β Scribed by Dwek, R. A.; Wain-Hobson, S.; Dower, S.; Gettins, P.; Sutton, B.; Perkins, S. J.; Givol, D.
- Book ID
- 109704016
- Publisher
- Nature Publishing Group
- Year
- 1977
- Tongue
- English
- Weight
- 585 KB
- Volume
- 266
- Category
- Article
- ISSN
- 0028-0836
- DOI
- 10.1038/266031a0
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## Conformational flexibility of an antibody combining site composed of two identical V regions" The variable portion of the light chain (VL) of protein 3 15 was studied as a model for antibody composed of two "like" chains. VL exists as a dimer which contains the binding subsite for the dinitrophe
## Abstract Using Xβray crystallography, a human monoclonal IgM cryoglobulin (Mez) was found to have an unusual combining site topography. Analysis of the unliganded Fv at 2.6β Γ resolution revealed that the HCDR3 had partitioned the active site into two compartments [Ramsland PA __et al.__ 2000. __