Changing Tryptophan (Trp, W) to Asparagine (Asn, N)
Average differences for changing Tryptophan (Trp, W) to Asparagine (Asn, N)
Values are log-odds differences when comparing the two amino acids (second - first). The values for each amino acid are in the images below. High (green) values indicate changes that are favored by the mutations, low (red) values are
those disfavored (i.e. favored by the wild type). Note that these values do not mean that a change will induce or disrupt binding to the elements above necessarily. Whether the
impact is felt depends on what the particular amino acid position actually does. For instance, the DNA-binding values would apply if you think that the position of interest is at or
near a DNA binding site.
Side-chain interaction preferences (Protein, DNA, RNA, chemicals) for the wild-type residue (Trp)
Values are log-odds of how many contacts are seen in a set of non-redundant protein structures against how many would be expected randomly. P=protein, Chem=chemical, intra=within proteins, inter=between proteins, PTM=post-translational modificaitons, for DNA and RNA standard one-letter (ATCGU) codes used, ac=h-bond acceptor, do=h-bond donor, im=imidazole, py=pyrimidine
Side-chain interaction preferences (Protein, DNA, RNA, chemicals) for the mutated residue (Asn)
Values are log-odds of how many contacts are seen in a set of non-redundant protein structures against how many would be expected randomly. P=protein, Chem=chemical, intra=within proteins, inter=between proteins, PTM=post-translational modificaitons, for DNA and RNA standard one-letter (ATCGU) codes used, ac=h-bond acceptor, do=h-bond donor, im=imidazole, py=pyrimidine
Known changes of Tryptophan (Trp, W) to Asparagine (Asn, N)
Data from UniProt.
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Citation:
M.J. Betts, R.B. Russell. Amino acid properties and consequences of subsitutions.
In Bioinformatics for Geneticists, M.R. Barnes, I.C. Gray eds, Wiley, 2003.
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Author: Rob Russell, Heidelberg University