Global Journal of Medical Research, F: Diseases, Volume 22 Issue 4

rs199536408Glycine into a Aspartic Acid at position 198 The mutant residue is bigger and probably will not fit. Glycine is flexible enough to make these torsion angles, mutation into another residue will force the local backbone into an incorrect conformation and will disturb the local structure. rs375283568Glutamic Acid into a Lysine at position 168 The damaging effect is due to mutant residue is bigger than the wild-type and is locatedin a domain that is important for the main activity of the protein this residue might disturb this function rs143267384 Tryptophan into a Valine at position 60 The damaging effect is since, the mutation is found in a conserved region of the protein and important for its activity. The mutant residue is smaller than the wild residue, causing an empty space in the core of the protein. rs200808744Arginine into a Glutamine at position 53 The mutant residue is smaller than the wild-type residue. This will cause a possible loss of external interactions. There is also difference in the charge between the wild and mutant type.Mutation of the residue might disturb this function rs373921680Glutamic Acid into a Alanine at position 42 Only this residue type was found at this position. The damaging effect is due to decrease of wild-type residue size lead to loss of interactions with other molecules or residues. Decrease hydrophobicity of the mutant residue leading to loss of Hydrophobic interactions. rs199536408 Alanine into a Aspartic Acid at position 41 The damage may come from the fact that the mutation is at a highly conserved region. The mutant type is bigger than the wild one. It is also negatively charged while the wild is neutral. The residue is located on the surface of the protein, mutation of this residue can disturb interactions with other molecules or other parts of the protein. The mutation might cause loss of hydrophobic interactions with other molecules on the surface of the protein. 21 Year 2022 Global Journal of Medical Research Volume XXII Issue IV Version I ( D ) F © 2022 Global Journals Computational Analysis of Possibly Pathogenic Non-Synonymous Single Nucleotide Polymorphisms Variants in HGD Gene lycine into a Glutamic Acid at position 11 The damaging effect is due to mutant residue is bigger and probably will not fit. Glycine is flexible enough to make these torsion angles, mutation into another residue will force the local backbone into an incorrect conformation. charge, this can disrupts the local structure. *Note Grey colour: protein chains, red colour atoms are the wild amino acid residues, green are the mutated amino acids