Mangels C, Kellner R, Einsiedel J, Weiglmeier PR, Rösch P, Gmeiner P, Schwarzinger S (2010)
Publication Type: Journal article, Original article
Publication year: 2010
Original Authors: Mangels C., Kellner R., Einsiedel J., Weiglmeier P.R., Rosch P., Gmeiner P., Schwarzinger S.
Publisher: Taylor & Francis
Book Volume: 28
Pages Range: 13-22
Journal Issue: 1
DOI: 10.1080/07391102.2010.10507340
Antibodies have become indispensable reagents with numerous applications in biological and biotechnical analysis, in diagnostics as well as in therapy. In all cases, selective interaction with an epitope is crucial and depends on the conformation of the paratope. While epitopes are routinely mapped at high throughput, methods revealing structural insights on a rather short timescale are rare. We here demonstrate paramagnetic relaxation-enhanced (PRE) NMR spectroscopy to be a powerful tool unraveling structural information about epitope-orientation in a groove spanned by the complementary determining regions. In particular, we utilize the spin label TOAC, which is fused to the peptidic epitope using standard solid-phase chemistry and which is characterized by a reduced mobility compared to, e.g., spin labels attached to the side-chain functionalities of cysteine or lysine residues. We apply the method to determine the orientation of helix 1 of the prion protein, which is the epitope for the therapeutically anti-prion active scF fragment W226. ©Adenine Press (2010).
APA:
Mangels, C., Kellner, R., Einsiedel, J., Weiglmeier, P.R., Rösch, P., Gmeiner, P., & Schwarzinger, S. (2010). The therapeutically anti-prion active antibody-fragment scF v-W226: Paramagnetic relaxation-enhanced NMR spectroscopy aided structure elucidation of the paratope-epitope interface. Journal of Biomolecular Structure & Dynamics, 28(1), 13-22. https://doi.org/10.1080/07391102.2010.10507340
MLA:
Mangels, Christian, et al. "The therapeutically anti-prion active antibody-fragment scF v-W226: Paramagnetic relaxation-enhanced NMR spectroscopy aided structure elucidation of the paratope-epitope interface." Journal of Biomolecular Structure & Dynamics 28.1 (2010): 13-22.
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