Unknown

Dataset Information

0

Catch bond-like kinetics of helix cracking: network analysis by molecular dynamics and milestoning.


ABSTRACT: The first events of unfolding of secondary structure under load are considered with Molecular Dynamics simulations and Milestoning analysis of a long helix (126 amino acids). The Mean First Passage Time is a non-monotonic function of the applied load with a maximum of 3.6 ns at about 20 pN. Network analysis of the reaction space illustrates the opening and closing of an off-pathway trap that slows unfolding at intermediate load levels. It is illustrated that the nature of the reaction networks changes as a function of load, demonstrating that the process is far from one-dimensional.

SUBMITTER: Kreuzer SM 

PROVIDER: S-EPMC3716791 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Catch bond-like kinetics of helix cracking: network analysis by molecular dynamics and milestoning.

Kreuzer Steven M SM   Moon Tess J TJ   Elber Ron R  

The Journal of chemical physics 20130901 12


The first events of unfolding of secondary structure under load are considered with Molecular Dynamics simulations and Milestoning analysis of a long helix (126 amino acids). The Mean First Passage Time is a non-monotonic function of the applied load with a maximum of 3.6 ns at about 20 pN. Network analysis of the reaction space illustrates the opening and closing of an off-pathway trap that slows unfolding at intermediate load levels. It is illustrated that the nature of the reaction networks c  ...[more]

Similar Datasets

| S-EPMC4624728 | biostudies-literature
| S-EPMC5501303 | biostudies-literature
| S-EPMC3406243 | biostudies-literature
| S-EPMC5656527 | biostudies-literature
| S-EPMC9277580 | biostudies-literature
| S-EPMC3838425 | biostudies-other
| S-EPMC6107302 | biostudies-literature
| S-EPMC3218086 | biostudies-other
| S-EPMC7809013 | biostudies-literature
| S-EPMC6443090 | biostudies-literature