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Results: 6

1.
Figure 3

Figure 3. Unfolding of Fibrinogen In Silico. From: Mechanism of Fibrin(ogen) Forced Unfolding.

(A and B) Representative force-extension profiles for fibrinogen monomer Fg (A) and dimer Fg2 (B), respectively, obtained at a pulling velocity vf = 1.0 μm/s. All the curves that appear above the lowest curve are offset for clarity.
(C and D) Plots show the peak-to-peak distances and peak forces for the transitions of type 1–3 (see Figure S2 and Table S3). The peaks corresponding to these transitions are numbered as 1, 2, and 3 in the force spectra (A and B). A movie detailing the unfolding transitions in the dimer Fg2 is in Movie S1.

Artem Zhmurov, et al. Structure. ;19(11):1615-1624.
2.
Figure 5

Figure 5. Forced Unfolding of the Fibrin(ogen) D-Dimer In Silico (See Also Figure S3). From: Mechanism of Fibrin(ogen) Forced Unfolding.

(A) D-dimer undergoing the conformational transition from the “closed” state (structure 0) to the “open” state (structure 1).
(B) A force-extension profile for the D-dimer obtained at a pulling velocity vf = 1.0 mm/s. Disruption of the D-D junction is characterized by the weak first peak ( ~50 pN) and short chain extension ( ~3–5 nm). Also shown are the peak-to-peak distances and peak forces for transitions of type 1–3 (see Figure S2 and Table S3).

Artem Zhmurov, et al. Structure. ;19(11):1615-1624.
3.
Figure 6

Figure 6. Forced Unfolding of the Central Nodule of Fibrin(ogen)’s E Region. From: Mechanism of Fibrin(ogen) Forced Unfolding.

(A) Representative structures of the central nodule prior (structure 0) and after (structure 1) the unfolding transition.
(B) The time-dependence of the mechanical tension in the central nodule (solid curve; left y axis), and its extension along the direction of pulling force (dashed curve; right y axis), quantified by the distance between the two γ23Cys residues of the opposite γ chains. A sudden ~7 nm jump in the extension, observed at ~0.095 s, is due to the central domain unfolding. The inset shows the fibrin(ogen) structure with the central nodule and the adjacent coiled-coil regions.

Artem Zhmurov, et al. Structure. ;19(11):1615-1624.
4.
Figure 1

Figure 1. Human Fibrinogen Structure (PDB Entry: 3GHG). From: Mechanism of Fibrin(ogen) Forced Unfolding.

(A) A schematic representation of the Fg molecule in the naturally folded and fully unfolded states. The molecule is constrained at the C-terminal part of one γ chain (γIle394), and the mechanical force (f) is applied to the C-terminal part of the other γ chain (gGly395).
(B) Structural details showing the central nodule, γ-nodules, β-nodules, disulfide rings, and the γ-γ-crosslinking sites. Dimensions are shown as in the compact crystal structure, and the contour lengths of various structural elements are shown in the fully unfolded state assuming a contour length per residue of 0.38 nm.

Artem Zhmurov, et al. Structure. ;19(11):1615-1624.
5.
Figure 4

Figure 4. Forced Unfolding of the Fibrin(ogen) γ-Nodule In Silico. From: Mechanism of Fibrin(ogen) Forced Unfolding.

(A–C) Panels show force-extension profiles for the γ-nodule alone (A), for the γ-nodule and adjacent portion of the β-chain (B), and for the complex of the γ- and β-nodules (C). In each structure, the simulated portion is colorized, and the “truncated” portion, not used in the simulations, is shown in gray. The force peaks correspond to the transitions of type 1–3 (see Table S3).
(D) The unfolding steps and intermediate conformations observed for the γ-nodule. Structures 0, 1, 2a, 2b, and 3 correspond to the accordingly numbered force peaks in the force-distance curves (A–C). Also shown are the maximal extensions, corresponding to the peak-to-peak distances in the force-distance curves (see Figure S2).

Artem Zhmurov, et al. Structure. ;19(11):1615-1624.
6.
Figure 2

Figure 2. Unfolding of Fibrinogen In Vitro with AFM. From: Mechanism of Fibrin(ogen) Forced Unfolding.

(A and B) Experimental force-distance curves obtained at a pulling velocity vf = 1.0 mm/s for fibrinogen monomer Fg (A) and oligomers Fgn (B). See Figure S1 for more examples. All the curves that appear above the lowest curve are offset for clarity. In this figure and in Figures 3A and 3B, Figures 4A–4C, and Figure 5B the smooth overlaying curves represent numerical fits obtained using the wormlike chain model.
(C and D) The histograms of the peak-to-peak distances (number of data points n = 186) and peak forces (n = 226) are shown in (C) and (D), respectively. The bin size (Δx ≈ 6 nm and Δf ≈ 15.5 pN) has been estimated using the Freedman-Diaconis rule for optimal bandwidth selection (Bura et al., 2009). In (C), the solid curve represents the superposition of three Gaussian probability densities of unfolding forces (dashed lines) for the transitions of type 1, 2, and 3, displayed in Figure 3.

Artem Zhmurov, et al. Structure. ;19(11):1615-1624.

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