Evidence map›Paper›PMID 23259771›Full record

ArticleThe journal of physical chemistry. B2013

Extracting conformational memory from single-molecule kinetic data.

Steve Pressé, Julian Lee, Ken A Dill

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed.

  1. Single-molecule reaction-diffusion.Biophysical journal · 2025
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  4. Single-Molecule Reaction-Diffusion.bioRxiv : the preprint server for biology · 2023
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  15. Directly measuring single-molecule heterogeneity using force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2016
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Steve PresséDepartment of Physics, Indiana University-Purdue University, Indianapolis, Indiana, USA.
Julian Lee
Ken A Dill

Funding

COMBINATORIAL STATISTICAL MECHANICS OF PROTEIN FOLDINGR01GM034993 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DILL, KEN A · 1985 to 2009
$2.7M
NIGMS NIH HHS GM09025NIGMS NIH HHS GM34993NIGMS NIH HHS R01 GM034993
6 · The paper itself

Abstract

Single-molecule data often come in the form of stochastic time trajectories. A key question is how to extract an underlying kinetic model from the data. A traditional approach is to assume some discrete state model, that is, a model topology, and to assume that transitions between states are Markovian. The transition rates are then selected according to which ones best fit the data. However, in experiments, each apparent state can be a broad ensemble of states or can be hiding multiple interconverting states. Here, we describe a more general approach called the non-Markov memory kernel (NMMK) method. The idea is to begin with a very broad class of non-Markov models and to let the data directly select for the best possible model. To do so, we adapt an image reconstruction approach that is grounded in maximum entropy. The NMMK method is not limited to discrete state models for the data; it yields a unique model given the data, it gives error bars for the model, and it does not assume Markov dynamics. Furthermore, NMMK is less wasteful of data by letting the entire data set determine the model. When the data warrants, the NMMK gives a memory kernel that is Markovian. We highlight, by numerical example, how conformational memory extracted using this method can be translated into useful mechanistic insight.

Indexed as

Models, TheoreticalEntropyKineticsMarkov Chains

Identifiers

PMID23259771
PMCPMC3569860

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.