1. Volume 114, Issue 2, Pages 323-330 (January 2018)
Destabilizing the AXH Tetramer by Mutations: Mechanisms and Potential Antiaggregation Strategies 
Gianvito Grasso, Umberto Morbiducci, Diana Massai, Jack A. Tuszynski, Andrea Danani, Marco A. Deriu 
Biophysical Journal 
Volume 114, Issue 2, Pages (January 2018)
DOI: /j.bpj
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2. Figure 1
Visual inspection of the AXH-WT (a) and AXH-I580A (b) conformational arrangement at the equilibrium (left). The RMSF is reported in the right panel and represented on the protein 3D structure (center). To see this figure in color, go online.
Biophysical Journal  , DOI: ( /j.bpj )
Copyright © 2017 Biophysical Society Terms and Conditions

3. Figure 2
(a) Backbone RMSD (top) and rotation between dimers AB and CD described the cos(α) (bottom) throughout the overall MD simulation for wild-type and mutated protein. (b) Given here is a visual inspection of the molecular systems at the equilibrium in the cases of AXHt-WT (I) and AXHt-I580A system (II). (c) The scheme illustrates that the main structural modifications are characterized by a relative rotation between dimers AB and CD. To see this figure in color, go online.
Biophysical Journal  , DOI: ( /j.bpj )
Copyright © 2017 Biophysical Society Terms and Conditions

4. Figure 3
(a) RDF of the amine nitrogen atoms of the guanidinium group with respect to the backbone carbonyl oxygens of the interacting arginine residue. Only R638B and R638C are considered for the calculation. Two different peaks at 2.8 and 4.7 Å can be identified. The first peak is related to the primary interaction resulting from the hydrogen bond between the amine hydrogen atoms and the backbone oxygen, whereas the second peak indicates the water-mediated hydrogen bonding (59). The hydrogen bonds between the R638B and R638C residues are also represented in (b) and (c). To see this figure in color, go online.
Biophysical Journal  , DOI: ( /j.bpj )
Copyright © 2017 Biophysical Society Terms and Conditions

5. Figure 4
Free energy profile (kilojoules per moles) of the AXHt-WT, AXHt-I580A, and AXHt-R638A molecular systems, represented as a function of two collective variables: the AXH dimer-dimer distance and the cosine of the angle between vectors connecting two distinct AXH regions per dimer. To see this figure in color, go online.
Biophysical Journal  , DOI: ( /j.bpj )
Copyright © 2017 Biophysical Society Terms and Conditions