Abstract
Nucleotide evolution models benefit a lot from the reported neighbor-dependent nucleotide mutations. Investigations of neighboring-site effects of amino acid substitutions may also promote the development of protein evolution models. Here, the neighboring-site effects of amino acid substitutions in the mouse genome are evaluated by grouping the 20 amino acids into four categories: nonpolar neutral (NON), polar neutral (NEU), positive (POS) and negative (NEG) amino acids. Our data indicate that amino acid substitutions are evidently neighboring-site dependent, and the most prominent bias is the NEG→NEG substitution occurring in NEG_NEG context, the frequency of which is 2-fold higher than that of expectation. The neighboring-site effects are also correlated with some types of protein secondary structures. Through this study, we conclude that like neighbor-dependent nucleotide mutations, amino acid substitutions are also neighboring-site dependent. The mutation bias of nucleotide sequence and natural or functional selection on protein structure might be two underlying reasons for the neighboring-site effects of amino acid substitutions in the mouse genome.
Keywords: Amino acid substitution, C- and N-terminal, mice genome, neighboring-site, preference, second protein structure.
Related Books
In Vitro Propagation and Secondary Metabolite Production from Medicinal Plants: Current Trends (Part 2)
Micropropagation of Medicinal Plants
Software and Programming Tools in Pharmaceutical Research
Biotechnology and Drug Development for Targeting Human Diseases
In Vitro Propagation and Secondary Metabolite Production from Medicinal Plants: Current Trends (Part 1)
Molecular and Physiological Insights into Plant Stress Tolerance and Applications in Agriculture- Part 2
Micropropagation of Medicinal Plants
Genome Editing in Bacteria (Part 1)
Data Science for Agricultural Innovation and Productivity
Animal Models In Experimental Medicine
26
1