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Simulated Protein Thermal Detection (SPTD) for Enzyme Thermostability Study and an Application Example for Pullulanase from Bacillus deramificans

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Background: The relationship between protein structure and its bioactivity is one of the fundamental problems for protein engineering and pharmaceutical design.

Method: A new method, called SPTD (Simulated Protein Thermal Detection), was proposed for studying and improving the thermal stability of enzymes. The method was based on the evidence observed by conducting the MD (Molecular Dynamics) simulation for all the atoms of an enzyme vibrating from the velocity at a room temperature (e.g., 25°C) to the desired working temperature (e.g., 65°C). According to the recorded MD trajectories and the coordinate deviations of the constituent residues under the two different temperatures, some new strategies have been found that are useful for both drug delivery and starch industry.

Conclusion: The SPTD technique presented in this paper may become a very useful tool for pharmaceutical design and protein engineering.
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Keywords: B-factors; Simulated protein thermal detection; molecular dynamics; protein engineering; pullulanase; site-directed mutation; thermal stability

Document Type: Review Article

Publication date: September 1, 2018

This article was made available online on December 18, 2018 as a Fast Track article with title: "Simulated Protein Thermal Detection (SPTD) for Enzyme Thermostability Study and an Application Example for Pullulanase from Bacillus deramificans".

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