Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4697
Title: Peptide-protein interactions studied by surface plasmon and nuclear magnetic resonances.
Authors: Spiga, Ottavia 
Bernini, Andrea 
Scarselli, M.
Ciutti, A.
Bracci, Luisa
Lozzi, Luisa
Lelli, B.
DI MARO, D.
Calamandrei, D.
Niccolai, Neri 
Issue Date: 2002
Project: None 
Journal: FEBS LETTERS
Abstract: 
The structural features of the complexes that alpha-bungarotoxin forms with three different synthetic peptides, mimotopes of the nicotinic acetylcholine receptor binding site, have been compared to the corresponding nuclear magnetic resonance (NMR) and surface plasmon resonance (SPR) data. For the considered peptides, the observed different affinities towards the toxin could not be accounted simply by static structural considerations. A combined analysis of the SPR- and NMR-derived dynamic parameters shows new correlations between complex formation and dissociation and the overall pattern of intramolecular and intermolecular nuclear Overhauser effects. These features could be crucial for a rational design of protein ligands.
Description: 
35473
URI: http://hdl.handle.net/20.500.12779/4697
ISSN: 0014-5793
DOI: 10.1016/S0014-5793(01)03274-4
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