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- W2912556111 abstract "Apolipoprotein E4 is the strongest risk factor for Alzheimer's disease while the ApoE3 is considered normal and the ApoE2 is protective. ApoE3(112C) and ApoE4(112R) differ by one amino acid change at 112th position. Structure of ApoE consists of two domains, a 22 kDa N-terminal domain (1-167) and a 10 kDa C-terminal domain (238-299), connected by a hinge region. Here we investigate the role of the amino acid at position 112 on the stability and the domain-domain interactions by performing substitution of C112 to different amino acids of varying hydrophobicity. Our results indicate that stability of the N-terminal domain increases dramatically with increasing hydrophobicity of the residue at 112. Intramolecular Fosters Resonance Energy Transfer (FRET) between N- and the C-terminal domains indicate that the stability of the domain-domain interactions is correlated with the stability of the N-terminal domain. Furthermore, presence of the C-terminal domain destabilizes the N-terminal domains of ApoE4 but not ApoE3. Taken together our data indicate that nature of the residue at position 112 plays strong role on both the stability and the domain-domain interactions in ApoE." @default.
- W2912556111 created "2019-02-21" @default.
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- W2912556111 date "2019-02-01" @default.
- W2912556111 modified "2023-10-18" @default.
- W2912556111 title "Biophysical Characterization of Differences in Domain-Domain Interactions between the Apolipoprotein E4 and E3" @default.
- W2912556111 doi "https://doi.org/10.1016/j.bpj.2018.11.1066" @default.
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