histograms fit with gaussian curves  (GraphPad Software Inc)

Journal: Biophysical Journal

Article Title: Phosphorylating Titin’s Cardiac N2B Element by ERK2 or CaMKII δ Lowers the Single Molecule and Cardiac Muscle Force

doi: 10.1016/j.bpj.2015.11.002

Figure Lengend Snippet: Single-molecule mechanics on titin’s N2B element. (A) Schematic of an N2B molecule tethered between a microscope slide and cantilever tip. (B) Example of a force-extension curve of the N2B molecule. Three force peaks are present due to Ig domain unfolding, and a fourth peak represents the molecule breaking loose from the cantilever. Force curves were fit by the WLC equation; contour length (Lc) values are shown in the inset. The Lc of the first peak is due to the N2B-Us, and the subsequent Lc values indicate gains due to Ig domain unfolding. (C) Lc histogram of N2B-US. (D) Persistence length (Lp) histogram of N2B-Us. (E) Unfolding force (Uf) of Ig domains. Results were fit by Gaussian curves; peaks are shown on the graph. To see this figure in color, go online.

Article Snippet: Values were also plotted in histograms that were fit with Gaussian curves (GraphPad Prism).

Techniques: Microscopy

Journal: Biophysical Journal

Article Title: Phosphorylating Titin’s Cardiac N2B Element by ERK2 or CaMKII δ Lowers the Single Molecule and Cardiac Muscle Force

doi: 10.1016/j.bpj.2015.11.002

Figure Lengend Snippet: (A and B) Effect of CaMKIIδ (A) and ERK2 (B) on the Lp of N2B-Us. After phosphorylation, the Lp distribution is shifted to the right from that of unphosphorylated molecules (indicated by broken curves; same data as in Fig. 1). The values shown are peak positions of Gaussian fits.

Article Snippet: Values were also plotted in histograms that were fit with Gaussian curves (GraphPad Prism).

Techniques: Phospho-proteomics

Journal: Biophysical Journal

Article Title: Phosphorylating Titin’s Cardiac N2B Element by ERK2 or CaMKII δ Lowers the Single Molecule and Cardiac Muscle Force

doi: 10.1016/j.bpj.2015.11.002

Figure Lengend Snippet: Effect of ERK2 on N2B-Us measured under oxidizing conditions. (A) Left: N2B-Us with its six cysteines (red font) and the three ERK2 phospho-sites (blue font). Right: all possible cross-link combinations between the six cysteines, showing the number of residues in between the cross-links and the effect of cross-linking on the Lc of the N2B-Us (shown in parentheses and calculated assuming that each reduces the Lc by 0.35 nm). (B–D) Measurements obtained under oxidizing conditions (no DTT). (B) Lc of N2B-Us. The Lc distribution can be fit with a double Gaussian with peaks at 107 and 195 nm. Broken curve: measurements under reducing conditions (from Fig. 1B). The difference in peak positions (88 nm) can be explained by cross-linking between either the first and third or the second and fourth cysteines (indicated in red in (A), right). (C and D) ERK2 has no effect on the Lp. To see this figure in color, go online.

Article Snippet: Values were also plotted in histograms that were fit with Gaussian curves (GraphPad Prism).

Techniques: