Reference : 1H, 13C and 15N backbone resonance assignments of the β-lactamase BlaP from Bacillus ...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/216177
1H, 13C and 15N backbone resonance assignments of the β-lactamase BlaP from Bacillus licheniformis 749/C and two mutational variants
English
Kay, Jennifer mailto [Université de Liège - ULiège > Département des sciences de la vie > Enzymologie et repliement des protéines >]
Thorn, David mailto [> >]
Rhazi, Noureddine mailto [Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques >]
Dumoulin, Mireille mailto [Université de Liège - ULiège > Département des sciences de la vie > Département des sciences de la vie >]
Corazza, Alessandra mailto [> >]
Damblon, Christian mailto [Université de Liège - ULiège > Département de chimie (sciences) > Chimie biologique structurale >]
13-Oct-2017
Biomolecular NMR Assignments
Springer
Yes (verified by ORBi)
International
1874-2718
1874-270X
Dordrecht
Netherlands
[en] BlaP hybrid proteins ; Polyglutamine model proteins ; Protein aggregation ; Polyglutamine diseases ; Resonance assignment
[en] Class A β-lactamases have been widely used as versatile scaffolds to create hybrid (or chimeric) proteins for a series of applications ranging from basic research to medicine. We have, in particular, used the β-lactamase BlaP from Bacillus licheniformis 749/C (BlaP) as a protein scaffold to create model polyglutamine (polyQ) proteins in order to better understand the mechanism(s) by which an expanded polyQ sequence triggers the formation of amyloid fibrils. The model chimeras were designed by inserting a polyQ sequence of various lengths at two different locations within BlaP (i.e. position 197 or position 216) allowing a detailed comparison of the effects of subtle differences in the environment of the polyQ sequence on its ability to trigger protein aggregation. In order to investigate the effects of the polyQ insertion at both positions on the structure, stability and dynamics of BlaP, a series of NMR experiments including H/D exchange are foreseen. Accordingly, as necessitated by these studies, here we report the NMR assignment of the wild-type BlaP (BlaP-WT) and of the two reference proteins BlaP197Q0 and BlaP216Q0, wherein a dipeptide Pro-Gly has been introduced at position 197 and 216, respectively; this dipeptide originates from the addition of the Sma1 restriction site at the genetic level to allow further polyQ sequence insertion.
http://hdl.handle.net/2268/216177
10.1007/s12104-017-9782-3

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