Computational analysis of the effect of Gly100Ala mutation on the thermostability of SazCA

Abstract

Maintaining the protein stability upon mutation is a challenging task in protein engineering. In the present computational study, we induced a single point Gly100Ala mutation in SazCA and examined the factors governing the stability and flexibility of the mutated form, and compared it to that of the wildtype using molecular dynamics simulations. We observed higher structural stability and lesser residual mobility in the mutated SazCA. Improved H-bonding due to Gly100Ala was observed. Ala100 was responsible for the increased helical contents in the mutated SazCA while Gly100 compromised the secondary structure contents in the wildtype. A strong network of salt bridges and high local ordering of the solvent molecules at the protein surface contributed to the enhanced stability of the mutated protein. Our simulations conclusively highlight Gly100Ala mutation as a step towards designing a more robust and thermostable SazCA.

Communicated by Ramaswamy H. Sarma

Keywords:

• Sulfurihydrogenibium azorense
• mutation
• structural stability
• flexibility
• thermostability

Acknowledgment

The computational facilities provided by the Param Shakti-National Supercomputing Mission (NSM), Government of India, at Indian Institute of Technology Kharagpur are gratefully acknowledged.

Disclosure statement

No potential conflict of interest was reported by the authors.

Additional information

Funding

This work was supported by the Department of Biotechnology of Ministry of Science and Technology, Government of India (Bioinformatics, computational and systems biology programme BT/PR7054/BID/7/422/2012).