Evidence map›Paper›PMID 22733562›Full record

ArticleProteins2012

Event detection and sub-state discovery from biomolecular simulations using higher-order statistics: application to enzyme adenylate kinase.

Arvind Ramanathan, Andrej J Savol, Pratul K Agarwal, Chakra S Chennubhotla

Abstract read
In one paragraph

Article in Proteins, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. Visualizing Rev1 catalyze protein-template DNA synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2020
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  14. Review
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  16. Identifying localized changes in large systems: Change-point detection for biomolecular simulations.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  17. Article
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

4 authors.

Arvind RamanathanComputational Biology Institute & Computer Science and Mathematics Division, Oak Ridge National Laboratory, Oak Ridge, TN 37830, USA.
Andrej J Savol
Pratul K Agarwal
Chakra S Chennubhotla

Funding

Integrated Interdisciplinary, inter-university PhD Program Computational Biology (T32)T32EB009403 · NIBIB · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BAHAR, IVET, BAR-JOSEPH, ZIV · 2009 to 2023
$4.4M
Structural Dynamics of Biomolecular SystemsR01GM086238 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BAHAR, IVET · 2009 to 2012
$1.3M
Accelerating Biomolecular Simulations on Reconfigurable Computing HardwareR21GM083946 · NIGMS · UT-BATTELLE, LLC-OAK RIDGE NATIONAL LAB · PI AGARWAL, PRATUL K · 2008 to 2009
$409k
NIBIB NIH HHS T32 EB009403NIGMS NIH HHS GM083946NIGMS NIH HHS GM086238NIGMS NIH HHS R01 GM086238NIGMS NIH HHS R21 GM083946
6 · The paper itself

Abstract

Biomolecular simulations at millisecond and longer time-scales can provide vital insights into functional mechanisms. Because post-simulation analyses of such large trajectory datasets can be a limiting factor in obtaining biological insights, there is an emerging need to identify key dynamical events and relating these events to the biological function online, that is, as simulations are progressing. Recently, we have introduced a novel computational technique, quasi-anharmonic analysis (QAA) (Ramanathan et al., PLoS One 2011;6:e15827), for partitioning the conformational landscape into a hierarchy of functionally relevant sub-states. The unique capabilities of QAA are enabled by exploiting anharmonicity in the form of fourth-order statistics for characterizing atomic fluctuations. In this article, we extend QAA for analyzing long time-scale simulations online. In particular, we present HOST4MD--a higher-order statistical toolbox for molecular dynamics simulations, which (1) identifies key dynamical events as simulations are in progress, (2) explores potential sub-states, and (3) identifies conformational transitions that enable the protein to access those sub-states. We demonstrate HOST4MD on microsecond timescale simulations of the enzyme adenylate kinase in its apo state. HOST4MD identifies several conformational events in these simulations, revealing how the intrinsic coupling between the three subdomains (LID, CORE, and NMP) changes during the simulations. Further, it also identifies an inherent asymmetry in the opening/closing of the two binding sites. We anticipate that HOST4MD will provide a powerful and extensible framework for detecting biophysically relevant conformational coordinates from long time-scale simulations.

Indexed as

Molecular Dynamics SimulationAdenylate KinaseBinding SitesEscherichia coliProtein ConformationProtein Structure, TertiaryAdenylate Kinase

Identifiers

PMID22733562
PMCPMC3538151

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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.