Intrinsic Disorder-based Design of Stable Globular Proteins

Authors

• Galina S. Nagibina, Institute of Protein Research of the Russian Academy of Sciences
• Tatiana N. Melnik, Institute of Protein Research of the Russian Academy of Sciences
• Ksenia A. Glukhova, Institute of Protein Research of the Russian Academy of Sciences
• Vladimir N. Uversky, University of South FloridaFollow
• Bogdan S. Melnik, Institute of Protein Research of the Russian Academy of Sciences

Document Type

Book Chapter

Publication Date

2020

Keywords

Protein Stability, Intrinsically Disorder Propensity, Stable Mutant Proteins, Design of Disulfide Bond, Design of Protein Circular Permutant

Digital Object Identifier (DOI)

https://doi.org/10.1016/bs.pmbts.2020.05.005

Abstract

Directed stabilization of globular proteins via substitution of a minimal number of amino acid residues is one of the most complicated experimental tasks. In this work, we have successfully used algorithms for the evaluation of intrinsic disorder predisposition (such as PONDR® FIT and IsUnstruct) as tools for searching for the weakened regions in structured globular proteins. We have shown that the weakened regions found by these programs as regions with highest levels of predicted intrinsic disorder predisposition are a suitable target for introduction of stabilizing mutations.

Was this content written or created while at USF?

Yes

Citation / Publisher Attribution

Intrinsic Disorder-based Design of Stable Globular Proteins, in V. N. Uversky (Ed.), Progress in Molecular Biology and Translational Science, Academic Press, p. 157-186

Scholar Commons Citation

Nagibina, Galina S.; Melnik, Tatiana N.; Glukhova, Ksenia A.; Uversky, Vladimir N.; and Melnik, Bogdan S., "Intrinsic Disorder-based Design of Stable Globular Proteins" (2020). Molecular Medicine Faculty Publications. 1146.
https://digitalcommons.usf.edu/mme_facpub/1146