ArticleJournal of computational chemistry2012
Simulation of multiphase systems utilizing independent force fields to control intraphase and interphase behavior.
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.
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.
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.
Who cites it
10 citing papers in PubMed.
- Artificial intelligence driven molecule adsorption prediction (AIMAP) applied to chirality recognition of amino acid adsorption on metals.Chemical science · 2024Article
- Article
- Experimental characterization and simulation of amino acid and peptide interactions with inorganic materials.Engineering in life sciences · 2018Review
- Application of advanced sampling and analysis methods to predict the structure of adsorbed protein on a material surface.Biointerphases · 2017Article
- Predicting the orientation of protein G B1 on hydrophobic surfaces using Monte Carlo simulations.Biointerphases · 2016Article
- Force fields for simulating the interaction of surfaces with biological molecules.Interface focus · 2016Review
- Parameterization of an interfacial force field for accurate representation of peptide adsorption free energy on high-density polyethylene.Biointerphases · 2015Article
- Perspectives on the simulation of protein-surface interactions using empirical force field methods.Colloids and surfaces. B, Biointerfaces · 2014Article
- 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 · 2012Article
- Development of a tuned interfacial force field parameter set for the simulation of protein adsorption to silica glass.Biointerphases · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
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
Identifiers
What OpenQuestion holds
Registered trials
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.