Protein stability estimation using PoPMusic and CUPSAT revealed that variant Asp148Glu caused structural destabilizing effects on the APE1 protein structure.
It revealed that the amino acid alteration resulted in low levels of folding free energy (ΔΔ G = 1.16 kcal/mol) and caused structural destabilizing effects.
Results show that the thermal loading history effect is important for structural integrity of solid propellant grains, and improper negligence may cause structural failure of missile systems.
They are also liable to cause structural damage.
Lumbar and femoral bones were evaluated by using bone densitometry to determine whether in utero DES exposure caused structural changes and whether this effect was gender specific.
This effect was attributed to amino acid changes in CH1 that caused structural differences in the attached V region that translated into variations in antigen binding [11].
This variety causes structural uncertainty [ 55].
This result, observed in association with 21 variants, is highly suggestive of a variant causing a structural effect on the mutant protein, impairing secretion.
In our results, we observed that structural effects caused by SNPs in 5′- or 3′-UTR are similar to those caused by SNPs in protein coding region (fig. 3 D).
In other cases, structural effects caused by the chromosomal rearrangement might contribute to a phenotype (Ricard et al., 2010).
Hence, a systematic analysis of structural effects caused by exonic variants, including synonymous SNPs, nonsynonymous SNPs, SNPs in 5′-UTRs, and SNPs in 3′-UTRs will help provide insights into the functional and structural effects of rare exonic SNPs in the human genome.
