Please use this identifier to cite or link to this item: http://hdl.handle.net/2067/1786
Title: Redesigning the reactive site loop of the wheat subtilisin/chymotrypsin inhibitor (WSCI) by site-directed mutagenesis. A protein–protein interaction study by affinity chromatography and molecular modeling
Authors: Bruni, Natalia
Di Maro, Antimo
Costantini, Susan
Chambery, Angela
Facchiano, Angelo M.
Ficca, Anna Grazia
Parente, Augusto
Poerio, Elia
Keywords: E/I complexes;ESI Q-TOF mass spectrometry;Time-course proteolysis;WSCI mutants
Issue Date: 2009
Publisher: Elsevier
Source: Bruni, N. et al. 2009. Redesigning the reactive site loop of the wheat subtilisin/chymotrypsin inhibitor (WSCI) by site-directed mutagenesis. A protein–protein interaction study by affinity chromatography and molecular modeling. "Biochimie". 91, 1112-1122.
Abstract: 
A site-directed mutagenesis strategy was employed to obtain four mutants of wheat subtilisin/chymotrypsin inhibitor (WSCI), with the aim to produce inactive forms of this protein. The mutants were expressed in Escherichia coli as fusion proteins and, after the tag removal, were purified to homogeneity and characterized, for their interaction with the inhibited enzymes, by affinity chromatography and molecular modeling.

Al fine di ottenere forme inattive di un inibitore proteico della subtilisina e della chimotripsina, è stata impiegata una strategia di mutagenesi sito-specifica. Sono stati così ottenuti quattro prodotti di espressione eterologa (mutanti dell’inibitore WSCI) che dopo purificazione sono stati sottoposti ad ampia caratterizzazione. In particolare, loro interazione con alcuni enzimi proteolitici d’interesse è stata studiata mediante cromatografia di affinità e modellamento molecolare.
Description: 
L'articolo é disponibile sul sito dell'editore: http://www.sciencedirect.com
URI: http://hdl.handle.net/2067/1786
ISSN: 0300-9084
DOI: 10.1016/j.biochi.2009.05.010
Appears in Collections:DABAC - Archivio della produzione scientifica

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