Evidence map›Paper›PMID 15806388›Full record

ArticleJournal of molecular modeling2005

Computer simulation of polypeptide translocation through a nanopore.

Andrzej Sikorski, Piotr Romiszowski

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Journal of molecular modeling, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Computer simulation of polypeptides in a confinement.Journal of molecular modeling · 2007
    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

2 authors.

Andrzej SikorskiDepartment of Chemistry, University of Warsaw, Pasteura 1, 02-093, Warszawa, Poland.
Piotr Romiszowski

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A simplified model of polypeptide chains was designed and studied by means of computer simulations. Chains were represented by a sequence of united atoms located at the positions of the alpha-carbons. A further assumption was the lattice approximation for the chains. We used a (310) lattice, which was found useful for studying properties of proteins. The force field used consisted of a long-range contact potential between amino-acid residues and a local preference for forming alpha-helical states. The chain consisted of two kinds of residues: hydrophilic (P) and hydrophobic (H) ones forming model helical septets--HHPPHPP--in a sequence. The chains were placed near an impenetrable surface with a square hole in it. The size of the hole was comparable or smaller than the size of a chain. The properties of these model chains were determined using the Monte-Carlo simulation method. During the simulations, translocation of the chain through the hole in the wall was observed. The influence of the chain length, the temperature differences on both sides of the wall and the force field on the chain properties were investigated. It was shown that the translocation time scales as N(2.2) and it was found that the presence of the local helical potential significantly slows down the process of translocation. [Figure: see text]. The snapshots of typical chain's conformation obtained during the simulation for chain consisted of N = 60. The values of the local potential epsilon(loc) = -8.

Indexed as

Computer SimulationModels, BiologicalNanostructuresMonte Carlo MethodPeptidesPorosityProtein ConformationProtein TransportTemperatureTime FactorsPeptides

Identifiers

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.