Abstract
We present an effective method for estimating the motion of proteins from the motion of attached probe particles in single-molecule experiments. The framework naturally incorporates Langevin dynamics to compute the most probable trajectory of the protein. By using a perturbation expansion technique, we achieve computational costs more than 3 orders of magnitude smaller than the conventional gradient descent method without loss of simplicity in the computation algorithm. We present illustrative applications of the method using simple models of single-molecule experiments and confirm that the proposed method yields reasonable and stable estimates of the hidden motion in a highly efficient manner.
Original language | English |
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Article number | 135104 |
Journal | Journal of Chemical Physics |
Volume | 134 |
Issue number | 13 |
DOIs | |
Publication status | Published - 2011 Apr 7 |
Externally published | Yes |
ASJC Scopus subject areas
- Physics and Astronomy(all)
- Physical and Theoretical Chemistry
- Medicine(all)