Evidence map›Paper›PMID 22488548›Full record

ArticleJournal of computational chemistry2012

Simulation of multiphase systems utilizing independent force fields to control intraphase and interphase behavior.

Pradip K Biswas, Nadeem A Vellore, Jeremy A Yancey, Tugba G Kucukkal, Galen Collier, Bernard R Brooks, Steven J Stuart, Robert A Latour

Abstract read
In one paragraph

Article in Journal of computational chemistry, 2012. 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.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Peptide-surface adsorption free energy comparing solution conditions ranging from low to medium salt concentrations.Chemphyschem : a European journal of chemical physics and physical chemistry · 2012
    Article
  10. 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

8 authors.

Pradip K BiswasDepartment of Physics, Tougaloo College, Tougaloo, MS.
Nadeem A Vellore
Jeremy A Yancey
Tugba G Kucukkal
Galen Collier
Bernard R Brooks
Steven J Stuart
Robert A Latour

Funding

TOUGALOO PROTEOMICSP20RR016476 · NCRR · UNIVERSITY OF SOUTHERN MISSISSIPPI · PI SHEARER, GLEN · 2001 to 2011
$30.4M
RESBIO - the Technology Resource for Polymeric BiomaterialsP41EB001046 · NIBIB · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI KOHN, JOACHIM B. · 2003 to 2017
$17.0M
Development Of Theoretical Methods For Studying Biological MacromoleculesZIAHL001051 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI BROOKS, BERNARD R · 2009 to 2025
$16.2M
YBCO Coated Conductors for 25 Tesla NMR MagnetsR44EB000616 · NIBIB · AMERICAN SUPERCONDUCTOR CORPORATION · PI THIEME, CORNELIS L. · 2003 to 2004
$750k
Intramural NIH HHS ZIA HL001051NCRR NIH HHS P20RR016476NIBIB NIH HHS P41 EB001046NIBIB NIH HHS R01 EB00616NIBIB NIH HHS R44 EB000616
6 · The paper itself

Abstract

Fixed-charge empirical force fields have been developed and widely used over the past three decades for all-atom molecular simulations. Most simulation programs providing these methods enable only one set of force field parameters to be used for the entire system. Whereas this is generally suitable for single-phase systems, the molecular environment at the interface between two phases may be sufficiently different from the individual phases to require a different set of parameters to be used to accurately represent the system. Recently published simulations of peptide adsorption to material surfaces using the CHARMM force field have clearly demonstrated this issue by revealing that calculated values of adsorption free energy substantially differ from experimental results. Whereas nonbonded parameters could be adjusted to correct this problem, this cannot be done without also altering the conformational behavior of the peptide in solution, for which CHARMM has been carefully tuned. We have developed a dual-force-field approach (Dual-FF) to address this problem and implemented it in the CHARMM simulation package. This Dual-FF method provides the capability to use two separate sets of nonbonded force field parameters within the same simulation: one set to represent intraphase interactions and a separate set to represent interphase interactions. Using this approach, we show that interfacial parameters can be adjusted to correct errors in peptide adsorption free energy without altering peptide conformational behavior in solution. This program thus provides the capability to enable both intraphase and interphase molecular behavior to be accurately and efficiently modeled in the same simulation.

Indexed as

Molecular Dynamics SimulationAmino AcidsPeptidesProtein ConformationQuantum TheorySolutionsThermodynamicsAmino AcidsPeptidesSolutionsadsorption free energyCHARMMdual‐FFinterfacial force fieldpeptide adsorption

Identifiers

PMID22488548
PMCPMC4110183

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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.