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Title: Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope
Award ID(s):
1817556 1517245 1244297
NSF-PAR ID:
10095219
Author(s) / Creator(s):
; ; ; ;
Date Published:
Journal Name:
Journal of Visualized Experiments
Issue:
144
ISSN:
1940-087X
Format(s):
Medium: X
Sponsoring Org:
National Science Foundation
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  1. Abstract

    Although the phenomenon of residual force depression has been known for decades, the mechanisms remain elusive. In the present study, we investigated mechanisms of residual force depression by measuring the stiffness to force ratio during force redevelopment after shortening at different velocities. The results showed that the slope of the relationship between muscle stiffness and force decreased with decreasing shortening velocity, and the y-intercept increased with decreasing shortening velocity. The differing slopes and y-intercepts indicate that the stiffness to force ratio during isometric force redevelopment depends on the active shortening velocity at a given muscle length and activation level. The greater stiffness to force ratio after active shortening can potentially be explained by weakly-bound cross bridges in the new overlap zone. However, weakly-bound cross bridges are insufficient to explain the reduced slope at the slowest shortening velocity because the reduced velocity should increase the proportion of weakly- to strongly-bound cross bridges, thereby increasing the slope. In addition, if actin distortion caused by active shortening recovers during the force redevelopment period, then the resulting slope should be similar to the non-linear slope of force redevelopment over time. Alternatively, we suggest that a tunable elastic element, such as titin, could potentially explain the results.

     
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  2. null (Ed.)