Journal: Archives of biochemistry and biophysics

Article Title: CHARACTERIZING INTERACTION FORCES BETWEEN ACTIN AND PROTEINS OF THE TROPOMODULIN FAMILY REVEALS THE PRESENCE OF THE N-TERMINAL ACTIN-BINDING SITE IN LEIOMODIN

doi: 10.1016/j.abb.2017.12.005

Figure Lengend Snippet: Distribution of unbinding forces measured between G-actin and a) Tmod1, b) Tmod3, c) Tmod2, d) Tmod21-346, and e) Tmod2[L73D], respectively. Insets show representative retraction force-curves with specific protein-protein unbinding force peaks. Solid lines show a dynamic peak function model fits to the data presented in the histograms (Origin 9.0, OriginLab Corp., Northampton, MA) (R2>0.95). Lognormal peak function was used for unimodal distribution whereas Gaussian peak function was used for bimodal distributions. Peak values estimated from dynamic peak function fitting representing the most probable values are given as insets. Tmod2 shows bimodal distribution suggesting that multiple actin binding sites are involved in the interactions to G-actin. Note that peak value of Tmod21-346 (64.0±3.6) is similar to the first peak value of Tmod2 (60.3±1.5) (p>0.05). f) Retraction force curve measured between Tmod11-344[L71D] and G-actin. The interactions between Tmod11-344[L71D] and G-actin were purely repulsive displaying no specific or nonspecific interactions.

Article Snippet: Solid lines show a dynamic peak function model fits to the data presented in the histograms (Origin 9.0, OriginLab Corp., Northampton, MA) ( R 2 >0.95).

Techniques: Binding Assay

Journal: Archives of biochemistry and biophysics

Article Title: CHARACTERIZING INTERACTION FORCES BETWEEN ACTIN AND PROTEINS OF THE TROPOMODULIN FAMILY REVEALS THE PRESENCE OF THE N-TERMINAL ACTIN-BINDING SITE IN LEIOMODIN

doi: 10.1016/j.abb.2017.12.005

Figure Lengend Snippet: Distributions of specific unbinding forces measured between a) Lmod2, b) Lmod21-514, and c) Lmod21-201 isoforms and G-actin, respectively. Insets show representative retraction force-curves showing specific protein-protein unbinding force peaks. Solid lines show a dynamic peak function model fits to the data presented in the histograms (Origin 9.0, OriginLab Corp., Northampton, MA) (R2>0.95). Lognormal peak function was used for unimodal distribution whereas Gaussian peak function was used for bimodal or trimodal distributions. Peak values estimated from dynamic peak function fitting representing the most probable values are given as insets. Lmod2 shows a trimodal distribution whereas Lmod21-514 shows a bimodal distribution suggesting that multiple actin binding sites are involved in the interactions to G-actin. Note that the first peak values of Lmod2 (56.0±2.9) and Lmod21-514 (47.3±1.1) is similar to the peak value of Lmod21-201 (58.2±1.4). Similarly, second peak value of Lmod2 (85.6±2.9) is similar to the second peak value of Lmod21-514 (78.4±1.5). Slight shifts in the peak values could be due to synergistic effect of multiple sites on the unbinding forces.

Article Snippet: Solid lines show a dynamic peak function model fits to the data presented in the histograms (Origin 9.0, OriginLab Corp., Northampton, MA) ( R 2 >0.95).

Techniques: Binding Assay