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RMBLab

Protein Biophysical Chemistry Group

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Transthyretin Amyloidogenic Behavior. At nearly physiological conditions, native tetrameric TTR (A) can dissociate to non-native monomers (B) which in turn depending on its conformational stability, may undergo partial unfolding (C). These partial unfolding monomeric species can lead to aggregate formation and consequently amyloid assembly (D).
Representative TTR conformations from MD unfolding simulations obtained by hierarchical agglomerative clustering for WT-TTR (A) and L55P-TTR (B). The residue at the mutation site is represented with spheres: Leu55 is colored in green and Pro55 in light green. [in Protein Sci. 19(2) pp. 202-219]
Schematic representation of the TTR protofilament model. [in Protein Sci. 15(1), pp. 28-32]
Structural representation of the binding modes of ligands T4 (left pocket) and PCB (right pocket) inside TTR. The contour surface clipped view exposing the binding sites interior is radial-colored from center (red) to edge (blue) of the protein.
Application of Virtual Screening Methods Toward the Discovery of Functional Transthyretin Amyloid Inhibitors [in J. Chem. Inf. Model. 50 (10), pp 1806–1820]
Modeling of the Toll-like receptor 3 and a putative Toll-like receptor 3 antagonist encoded by the African swine fever virus. [in Protein Sci. 20(2), pp. 247-255]
Secondary structure changes of Transthyretin accompanying amyloid formation, monitored by circular dichroism.
NMR spectra of peptide chignolin, A. 1D 1H-NMR; B. 2D DQF-COSY; C. 2D TOCSY; D. 2D ROESY.