Been thinking of other ideas. DNA methlyation is one thing we need to rule out.
DNA methylation may affect the transcription of genes in two ways. First, the methylation of DNA itself may physically impede the binding of transcriptional proteins to the gene, and second, and likely more important, methylated DNA may be bound by proteins known as methyl-CpG-binding domain proteins (MBDs). MBD proteins then recruit additional proteins to the locus, such as histone deacetylases and other chromatin remodeling proteins that can modify histones, thereby forming compact, inactive chromatin, termed silent chromatin. This link between DNA methylation and chromatin structure is very important. In particular, loss of methyl-CpG-binding protein 2 (MeCP2) has been implicated in Rett syndrome; and methyl-CpG-binding domain protein 2 (MBD2) mediates the transcriptional silencing of hypermethylated genes in cancer.
However, the possibility of the problem to be after this process is also valid and in this idea the problem is not with the DNA, genes and epigenome but with the proteins - the things the genes make. This would be termed a protein post translational modification.
Ways in which it happens:
Glycosylation: Many proteins, particularly in eukaryotic cells, are modified by the addition of carbohydrates, a process called glycosylation. Glycosylation in proteins results in addition of a glycosyl group to either asparagine, hydroxylysine, serine, or threonine. Software for studying glycosylation by glycan structure prediction.
Acetylation: the addition of an acetyl group, usually at the N-terminus of the protein.
Alkylation: The addition of an alkyl group (e.g. methyl, ethyl).
Methylation: The addition of a methyl group, usually at lysine or arginine residues. (This is a type of alkylation.)
Biotinylation: Acylation of conserved lysine residues with a biotin appendage.
Glutamylation: Covalent linkage of glutamic acid residues to tubulin and some other proteins.
Glycylation: Covalent linkage of one to more than 40 glycine residues to the tubulin C-terminal tail of the amino acid sequence.
Isoprenylation: The addition of an isoprenoid group (e.g. farnesol and geranylgeraniol).
Lipoylation: The attachment of a lipoate functionality.
Phosphopantetheinylation, The addition of a 4’-phosphopantetheinyl moiety from coenzyme A, as in fatty acid, polyketide, non-ribosomal peptide and leucine biosynthesis.
Phosphorylation, the addition of a phosphate group, usually to serine, tyrosine, threonine or histidine.
Sulfation: The addition of a sulfate group to a tyrosine.
In terms of research we should start at the genetic level and then work up to see where the problem is. Although I’m in favour with a systems view of biology this is the only realistic way to look at it.
The more I think about it this could be VERY important!