Submit Manuscript  

Article Details

Intrinsic Disorder-Based Design of Stabilizing Disulphide Bridge in Gαo Protein

[ Vol. 23 , Issue. 2 ]


Galina S. Nagibina, Ulyana F. Tin, Anatoly S. Glukhov, Tatiana N. Melnik and Bogdan S. Melnik   Pages 176 - 184 ( 9 )


In this study, we have used an approach that allows us to determine in what region of the polypeptide chain of protein it is required to insert a disulphide bond in order to stabilize it. In our previous paper [Melnik et al., JBSD. 2012] it was proposed that to search for a “weak” site in the protein, it is possible to use programs (for example, PONDR-FIT and IsUnstruct) finding intrinsic disorder protein regions. We suggested that in structured globular proteins, such programs predict not protein regions in the polypeptide chain disordered under native conditions, but “weakened”, feebly stabilized ones. Accordingly, an artificial introduction of SS-bridges using mutations in such regions would reliably result in the protein stabilization. We have taken advantage of this approach to stabilize protein G o from Drosophila melanogaster. The designed SS-bridge increased by 4 degrees the melting temperature of one domain of protein G o.


Disulphide bridge, Differential scanning microcalorimetry, G o, Protein intrinsic disorder regions, Protein stability, SS-bridge.


Institute of Protein Research (Moscow office), Room 104, Vavilova Street 34, Moscow, GSP 1, 117334, Russia.

Graphical Abstract:

Read Full-Text article