Evidence map›Paper›PMID 23345138›Full record

ArticleJournal of computational chemistry2013

Advanced techniques for constrained internal coordinate molecular dynamics.

Jeffrey R Wagner, Gouthaman S Balaraman, Michiel J M Niesen, Adrien B Larsen, Abhinandan Jain, Nagarajan Vaidehi

Abstract read
In one paragraph

Article in Journal of computational chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

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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

6 authors.

Jeffrey R WagnerDivision of Immunology, Beckman Research Institute of the City of Hope, Duarte, California 91010, USA.
Gouthaman S Balaraman
Michiel J M Niesen
Adrien B Larsen
Abhinandan Jain
Nagarajan Vaidehi

Funding

Physics-based Simulation of Biological Structures(RMI)U54GM072970 · NIGMS · STANFORD UNIVERSITY · PI PANDE, VIJAY S · 2004 to 2013
$33.5M
GNEIMO: Generalized Internal Coordinate Molecular Dynamics MethodsR01GM082896 · NIGMS · BECKMAN RESEARCH INSTITUTE/CITY OF HOPE · PI VAIDEHI, NAGARAJAN · 2008 to 2011
$1.2M
NIGMS NIH HHS R01 GM082896NIGMS NIH HHS R01GM082896NIGMS NIH HHS U54 GM072970
6 · The paper itself

Abstract

Internal coordinate molecular dynamics (ICMD) methods provide a more natural description of a protein by using bond, angle, and torsional coordinates instead of a Cartesian coordinate representation. Freezing high-frequency bonds and angles in the ICMD model gives rise to constrained ICMD (CICMD) models. There are several theoretical aspects that need to be developed to make the CICMD method robust and widely usable. In this article, we have designed a new framework for (1) initializing velocities for nonindependent CICMD coordinates, (2) efficient computation of center of mass velocity during CICMD simulations, (3) using advanced integrators such as Runge-Kutta, Lobatto, and adaptive CVODE for CICMD simulations, and (4) cancelling out the "flying ice cube effect" that sometimes arises in Nosé-Hoover dynamics. The Generalized Newton-Euler Inverse Mass Operator (GNEIMO) method is an implementation of a CICMD method that we have developed to study protein dynamics. GNEIMO allows for a hierarchy of coarse-grained simulation models based on the ability to rigidly constrain any group of atoms. In this article, we perform tests on the Lobatto and Runge-Kutta integrators to determine optimal simulation parameters. We also implement an adaptive coarse-graining tool using the GNEIMO Python interface. This tool enables the secondary structure-guided "freezing and thawing" of degrees of freedom in the molecule on the fly during molecular dynamics simulations and is shown to fold four proteins to their native topologies. With these advancements, we envision the use of the GNEIMO method in protein structure prediction, structure refinement, and in studying domain motion.

Indexed as

Molecular Dynamics SimulationSoftwareAlgorithmsKineticsProteinsProtein Structure, SecondaryThermodynamicsProteins

Identifiers

PMID23345138
PMCPMC3835462

What OpenQuestion holds

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Registered trials

None linked

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.