The p.Gly375Asp mutation is predicted to be damaging by prediction programs (Polyphen‐2: probably damaging [1], SIFT: damaging [0], MutationTaster: disease causing [1]).
The amyloidogenicity of each mutation is predicted by computing a joint mutational landscape over WT and mutant sequences, and quantifying which sequence more readily forms amyloid according to its energetic weight within the ensemble.
The I102del mutation is predicted to locate to the centre of TM3 and to change the overall prediction of TM domain structure (data not shown).
Among them, the W51F mutation is predicted to be the most effective in increasing the oxidation potential of the protein.
In addition, the mutation is predicted to cause an alteration in the second structure, which impairs protein synthesis and enlarges sensitivity to aminoglycoside ototoxicity (Prezant et al., 1993).
b However, BI-2536 treatment of the SW-13 did not increase the transcription of CDKN1A, as it is mutant for p53 and the mutation is predicted to decrease p53 transactivation functions.
p.R149C (g.940C>T) mutation is predicted to destabilize the protein in both models.
This mutation is predicted to result in a non-functional protein.
By analogy to previous studies using mouse orthologs, this mutation is predicted to abolish kinase activity.
For Omp31, the point mutation is predicted to lead to a truncation in the protein.
However, by changing a G U pair into a G C pair, the mutation is predicted to stabilize this stem.
