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Current studies show that codon optimization can affect protein conformation and function and increase expression levels.
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These functions included signal transduction and transcription, cytoskeleton regulation, xenobiotic metabolism, apoptosis, lipidogenesis, protein conformation or transport and cell cycle.
The effect of non-synonymous variants on protein conformation and function was assessed using Sift [ 23], Polyphen2 [ 24] and functional analysis through hidden markov models (Fathmm, version 2.3) [ 25].
However, recent reports indicate that codon optimization can affect protein conformation and function, increase immunogenicity, and reduce efficacy.
A large amount of free cholesterol trafficking to the ER of macrophages increases cholesterol-induced lipid ordering of the ER membrane and perturbs membrane protein conformation and function, providing a plausible mechanism for the decrease in SERCA activity induced by loading of the membrane with free cholesterol (Li et al., 2004).
Silver nanoparticles can be complexed with the thiol HS– (Cys) or amine H2N– groups [61 63] of the proteins and through electrostatic interactions [64] that have less impact on protein conformation and function.
Synonymous SNPs may alter RNA secondary structures and can affect protein conformation and function [ 1].
Citrullination is the conversion of a protein's arginine residues to citrulline, resulting in a loss of charge and often abnormal protein conformation and function.
It has also been shown that TrxR1 inhibition can influence p53 protein conformation and function.
The added positive charged arginine may have significant impact on the protein conformation and function.
Either process can change protein conformation and function, along with activation of proteolysis or autophagy to remove damaged proteins [ 42– 42].
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