The Influences of Palindromes in mRNA on Protein Folding Rates

Author:

Li Ruifang1ORCID,Li Hong2ORCID,Yang Sarula1ORCID,Feng Xue1ORCID

Affiliation:

1. College of Physics and Electronic Information, Inner Mongolia Normal University, Hohhot 010022, China

2. School of Physical Science and Technology, Inner Mongolia University, Hohhot 010021, China

Abstract

Background:It is currently believed that protein folding rates are influenced by protein structure, environment and temperature, amino acid sequence and so on. We have been working for long to determine whether and in what ways mRNA affects the protein folding rate. A large number of palindromes aroused our attention in our previous research. Whether these palindromes do have important influences on protein folding rates and what’s the mechanism? Very few related studies are focused on these problems.Objective:In this article, our motivation is to find out if palindromes have important influences on protein folding rates and what’s the mechanism.Method:In this article, the parameters of the palindromes were defined and calculated, the linear regression analysis between the values of each parameter and the experimental protein folding rates were done. Furthermore, to compare the results of different kinds of proteins, proteins were classified into the two-state proteins and the multi-state proteins. For the two kinds of proteins, the above linear regression analysis were performed respectively.Results :Protein folding rates were negatively correlated to the palindrome frequencies for all proteins. An extremely significant negative linear correlation appeared in the relationship between palindrome densities and protein folding rates. And the repeatedly used bases by different palindromes simultaneously have an important effect on the relationship between palindrome density and protein folding rate.Conclusion:The palindromes have important influences on protein folding rates, and the repeatedly used bases in different palindromes simultaneously play a key role in influencing the protein folding rates.

Funder

National Natural Science Foundation of China

Natural Science Foundation of Inner Mongolia

Research Program of science and technology at Universities of Inner Mongolia Autonomous Region

Publisher

Bentham Science Publishers Ltd.

Subject

Biochemistry,General Medicine,Structural Biology

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