Extremophiles

, Volume 21, Issue 3, pp 419–444 | Cite as

Multifactorial level of extremostability of proteins: can they be exploited for protein engineering?

  • Debamitra Chakravorty
  • Mohd Faheem Khan
  • Sanjukta Patra
Original Paper
  • 421 Downloads

Abstract

Research on extremostable proteins has seen immense growth in the past decade owing to their industrial importance. Basic research of attributes related to extreme-stability requires further exploration. Modern mechanistic approaches to engineer such proteins in vitro will have more impact in industrial biotechnology economy. Developing a priori knowledge about the mechanism behind extreme-stability will nurture better understanding of pathways leading to protein molecular evolution and folding. This review is a vivid compilation about all classes of extremostable proteins and the attributes that lead to myriad of adaptations divulged after an extensive study of 6495 articles belonging to extremostable proteins. Along with detailing on the rationale behind extreme-stability of proteins, emphasis has been put on modern approaches that have been utilized to render proteins extremostable by protein engineering. It was understood that each protein shows different approaches to extreme-stability governed by minute differences in their biophysical properties and the milieu in which they exist. Any general rule has not yet been drawn regarding adaptive mechanisms in extreme environments. This review was further instrumental to understand the drawback of the available 14 stabilizing mutation prediction algorithms. Thus, this review lays the foundation to further explore the biophysical pleiotropy of extreme-stable proteins to deduce a global prediction model for predicting the effect of mutations on protein stability.

Keywords

Extreme-stability Thermostability pH stability Halostability Barostability Application Engineering Mutation 

Abbreviations

ΔGu

Difference in Gibbs free energy of stability

Ts

Stability temperature

ΔHm

Change in enthalpy

ΔCp

Change in heat capacity

Tm

Melting temperature

Notes

Acknowledgements

Debamitra Chakravorty and Mohd Faheem Khan acknowledge Indian Institute of Technology Guwahati for research fellowship and infrastructure facility for carrying out PhD work. Research funding by Council of Scientific and Industrial Research (CSIR), Government of India is acknowledged.

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Copyright information

© Springer Japan 2017

Authors and Affiliations

  • Debamitra Chakravorty
    • 1
  • Mohd Faheem Khan
    • 1
  • Sanjukta Patra
    • 1
  1. 1.Department of Biosciences and BioengineeringIndian Institute of Technology GuwahatiGuwahatiIndia

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