Evidence map›Paper›PMID 19633920›Full record

ReviewPhotosynthesis research

The MoD-QM/MM methodology for structural refinement of photosystem II and other biological macromolecules.

Eduardo M Sproviero, Michael B Newcomer, José A Gascón, Enrique R Batista, Gary W Brudvig, Victor S Batista

Abstract readReview
In one paragraph

Review in Photosynthesis research. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Effects of aligned α-helix peptide dipoles on experimental electrostatic potentials.Protein science : a publication of the Protein Society · 2017
    Article
  5. Review
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.

Eduardo M SprovieroDepartment of Chemistry, Yale University, P. O. Box 208107, New Haven, CT, 06520-8107, USA.
Michael B Newcomer
José A Gascón
Enrique R Batista
Gary W Brudvig
Victor S Batista

Funding

STRUCTURE/FUNCTION RELATIONS IN MEMBRANE PROTEINSR01GM032715 · NIGMS · YALE UNIVERSITY · PI BRUDVIG, GARY W · 1985 to 2010
$2.7M
ELECTRONIC STRUCTURE OF FE-OXO AND MN-OXO COMPLEXESR01GM043278 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI NOODLEMAN, LOUIS · 1991 to 2010
$2.7M
NIGMS NIH HHS 2R01-GM043278NIGMS NIH HHS GM32715NIGMS NIH HHS R01 GM032715NIGMS NIH HHS R01 GM043278PHS HHS BSF R08164
6 · The paper itself

Abstract

Quantum mechanics/molecular mechanics (QM/MM) hybrid methods are currently the most powerful computational tools for studies of structure/function relations and structural refinement of macrobiomolecules (e.g., proteins and nucleic acids). These methods are highly efficient, since they implement quantum chemistry techniques for modeling only the small part of the system (QM layer) that undergoes chemical modifications, charge transfer, etc., under the influence of the surrounding environment. The rest of the system (MM layer) is described in terms of molecular mechanics force fields, assuming that its influence on the QM layer can be roughly decomposed in terms of electrostatic interactions and steric hindrance. Common limitations of QM/MM methods include inaccuracies in the MM force fields, when polarization effects are not explicitly considered, and the approximate treatment of electrostatic interactions at the boundaries between QM and MM layers. This article reviews recent advances in the development of computational protocols that allow for rigorous modeling of electrostatic interactions in extended systems beyond the common limitations of QM/MM hybrid methods. We focus on the moving-domain QM/MM (MoD-QM/MM) methodology that partitions the system into many molecular domains and obtains the electrostatic and structural properties of the whole system from an iterative self-consistent treatment of the constituent molecular fragments. We illustrate the MoD-QM/MM method as applied to the description of photosystem II as well as in conjunction with the application of spectroscopically constrained QM/MM optimization methods, based on high-resolution spectroscopic data (extended X-ray absorption fine structure spectra, and exchange coupling constants).

Indexed as

Molecular Dynamics SimulationQuantum TheoryMacromolecular SubstancesPhotosystem II Protein ComplexSpectrum AnalysisWaterMacromolecular SubstancesPhotosystem II Protein ComplexWater

Identifiers

PMID19633920
PMCPMC2954272

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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.