Evidence map›Paper›PMID 16853854›Full record

ArticleThe journal of physical chemistry. B2005

Calculation of the entropy and free energy from monte carlo simulations of a peptide stretched by an external force.

Srinath Cheluvaraja, Hagai Meirovitch

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Article in The journal of physical chemistry. B, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Minimalist explicit solvation models for surface loops in proteins.Journal of chemical theory and computation · 2006
    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.

Srinath CheluvarajaDepartment of Computational Biology, University of Pittsburgh School of Medicine, W1058 BST, Pittsburgh, Pennsylvania 15261, USA.
Hagai Meirovitch

Funding

Methods for Calculating the Free Energy of ProteinsR01GM066090 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MEIROVITCH, HAGAI · 2002 to 2010
$1.5M
Computational Methods for ProteinsR01GM061916 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MEIROVITCH, HAGAI · 2001 to 2003
$550k
NIGMS NIH HHS R01 GM061916NIGMS NIH HHS R01 GM066090NIGMS NIH HHS R01 GM61916NIGMS NIH HHS R01 GM66090
6 · The paper itself

Abstract

Hypothetical scanning Monte Carlo (HSMC) is a method for calculating the absolute entropy, S, and free energy, F, from a trajectory generated by any simulation technique. HSMC was applied initially to fluids (argon and water) and later to peptides and self-avoiding walks on a lattice. In this paper we make a step further and apply it to a model of decaglycine (at T = 300 K) in vacuum with constant bond lengths where external stretching forces are exerted at the end points; the changes in S and F are calculated as the forces are increased. The molecule is placed initially in a helical structure, which is changed to an extended structure after a short simulation time due to the exerted forces. This study has relevance to problems in polymers (e.g., rubber elasticity) and to the analysis of experiments where individual molecules are stretched by atomic force microscopy (AFM), for example. The results for S and F are accurate and are significantly better than those obtained by the quasi-harmonic approximation and the local states method. However, the molecule is quite stiff due to the strong bond angle potentials and the extensions are small even for relatively large forces. Correspondingly, as the force is increased the decrease in the entropy is relatively small while the potential energy is enhanced significantly. Still, differences, TDeltaS, for different forces are obtained with very good accuracy of approximately 0.2 kcal/mol.

Indexed as

EntropyMonte Carlo MethodThermodynamicsComputer SimulationModels, ChemicalOligopeptidesPeptidesProtein ConformationStress, MechanicaldecaglycineOligopeptidesPeptides

Identifiers

PMID16853854
PMCPMC1540612

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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.