Next Article in Journal
Gut Microbiota in Patients with Different Metabolic Statuses: Moscow Study
Next Article in Special Issue
Contribution of the Oligomeric State to the Thermostability of Isoenzyme 3 from Candida rugosa
Previous Article in Journal
Genotype-Environment Interaction Shapes the Microbial Assemblage in Grapevine’s Phyllosphere and Carposphere: An NGS Approach
Previous Article in Special Issue
Thermostable Xylanase Production by Geobacillus sp. Strain DUSELR13, and Its Application in Ethanol Production with Lignocellulosic Biomass
Article Menu
Issue 4 (December) cover image

Export Article

Open AccessReview
Microorganisms 2018, 6(4), 97;

Thermophilic Proteins as Versatile Scaffolds for Protein Engineering

Department of Chemical and Biomolecular Engineering, New York University, 6 MetroTech Center, Brooklyn, NY 11201, USA
Authors to whom correspondence should be addressed.
Current address: Weill Cornell Medicine, 1300 York Avenue, New York, NY 10065, USA.
Received: 2 September 2018 / Revised: 23 September 2018 / Accepted: 23 September 2018 / Published: 25 September 2018
(This article belongs to the Special Issue Thermophiles and Thermozymes)
Full-Text   |   PDF [869 KB, uploaded 25 September 2018]   |  


Literature from the past two decades has outlined the existence of a trade-off between protein stability and function. This trade-off creates a unique challenge for protein engineers who seek to introduce new functionality to proteins. These engineers must carefully balance the mutation-mediated creation and/or optimization of function with the destabilizing effect of those mutations. Subsequent research has shown that protein stability is positively correlated with “evolvability” or the ability to support mutations which bestow new functionality on the protein. Since the ultimate goal of protein engineering is to create and/or optimize a protein’s function, highly stable proteins are preferred as potential scaffolds for protein engineering. This review focuses on the application potential for thermophilic proteins as scaffolds for protein engineering. The relatively high inherent thermostability of these proteins grants them a great deal of mutational robustness, making them promising scaffolds for various protein engineering applications. Comparative studies on the evolvability of thermophilic and mesophilic proteins have strongly supported the argument that thermophilic proteins are more evolvable than mesophilic proteins. These findings indicate that thermophilic proteins may represent the scaffold of choice for protein engineering in the future. View Full-Text
Keywords: thermophilic proteins; protein engineering; protein stability; evolvability thermophilic proteins; protein engineering; protein stability; evolvability

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Finch, A.J.; Kim, J.R. Thermophilic Proteins as Versatile Scaffolds for Protein Engineering. Microorganisms 2018, 6, 97.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Microorganisms EISSN 2076-2607 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top