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. Author manuscript; available in PMC: 2024 Jun 12.
Published in final edited form as: J Chem Inf Model. 2023 May 29;63(11):3567–3578. doi: 10.1021/acs.jcim.3c00414

Figure 3. Conformal analysis for the homodimers and hetero-dimers of SEVI and Aβ.

Figure 3.

The average secondary content of SEVI a) and Aβ c) peptide in monomer, homo-dimer, and hetero-dimer. Probability of each residue from SEVI b) and Aβ d) adopting unstructured, β-sheet, and helix formations in monomer, homodimer, and heterodimer. The probability distribution of inter-peptide backbone hydrogen bonds and contacts in the SEVI and Aβ homo-dimer and hetero-dimer e). The change ratio of accessible surface area per residue of SEVI (upper) and Aβ (bottom) in the hetero-dimer compared to in the SEVI and Aβ isolated monomer f).