MARTINI statistics

info info

Citations per year

Number of citations per year for the bioinformatics software tool MARTINI

Tool usage distribution map

This map represents all the scientific publications referring to MARTINI per scientific context
info info

Associated diseases

This word cloud represents MARTINI usage per disease context

Popular tool citations

chevron_left Dynamics prediction Membrane simulation chevron_right
Want to access the full stats & trends on this tool?


MARTINI specifications


Unique identifier OMICS_32703
Software type Application/Script
Interface Command line interface
Restrictions to use None
Operating system Unix/Linux
Computer skills Advanced
Stability Stable
Maintained Yes


No version available


  • person_outline Siewert Marrink

Publication for MARTINI

MARTINI citations


Molecular details of dimerization kinetics reveal negligible populations of transient µ opioid receptor homodimers at physiological concentrations

Sci Rep
PMCID: 5955887
PMID: 29769636
DOI: 10.1038/s41598-018-26070-8

[…] ture was removed and the remaining residues of H8 added so that each structure consisted of sequence residues 65 to 352. The martinize python script was used to coarse grain the structures within the MARTINI v2.2 force field–. A modified version of the elastic network was applied to maintain the receptor tertiary structure,. Specifically, a harmonic force was applied to all backbone (BB) bead pair […]


Extension of coarse grained UNRES force field to treat carbon nanotubes

J Mol Model
PMCID: 5920012
PMID: 29700628
DOI: 10.1007/s00894-018-3656-1

[…] ESidue (UNRES) force field with a CNT treated as a cylinder with infinite length. UNRES is a coarse-grained force field [–] for protein simulation, which, like other coarse-grained force fields, e.g. Martini [], is constantly being improved and extended to treat not only proteins, but also nucleic acids, sugars, and lipids []. Owing to the simplified representation, UNRES provides an about 1000-fo […]


Structures of monomeric and oligomeric forms of the Toxoplasma gondii perforin like protein 1

Sci Adv
PMCID: 5943054
PMID: 29750191
DOI: 10.1126/sciadv.aaq0762
call_split See protocol

[…] For coarse-grained simulations, the Martini v2.2 coarse grain force field was used (, ). Lennard-Jones interactions were shifted to zero between 0.9 and 1.1 nm. The electrostatic potential energy was shifted to zero between 0 and 1.1 nm […]


Closely related, yet unique: Distinct homo and heterodimerization patterns of G protein coupled chemokine receptors and their fine tuning by cholesterol

PLoS Comput Biol
PMCID: 5864085
PMID: 29529028
DOI: 10.1371/journal.pcbi.1006062

[…] ure contained residues from Val37 to Phe320. Finally, both CC chemokine receptor structures were minimized using the CHARMM36 force field [].Subsequently, the protein structures were converted to the Martini2.2 coarse-grained force field [] using martinize []. In order to enforce the secondary and tertiary structure, an elastic RubberBands force network was applied. RubberBands as established in W […]


Tailoring the Variational Implicit Solvent Method for New Challenges: Biomolecular Recognition and Assembly

Front Mol Biosci
PMCID: 5816062
PMID: 29484300
DOI: 10.3389/fmolb.2018.00013

[…] ward large-scale applications and eventually merge it with molecular dynamics simulations. Recently, we adapted VISM to produce solvation free energies for “martinized” proteins (Ricci et al., ). The MARTINI model is a well-established meso-scale force field for modeling large molecular systems, which replaces groups of atoms by interaction centers commonly referred to as “beads,” based on an appr […]


Membrane perturbing properties of toxin mycolactone from Mycobacterium ulcerans

PLoS Comput Biol
PMCID: 5814095
PMID: 29401455
DOI: 10.1371/journal.pcbi.1005972

[…] entire mycolactone with respect of the center of mass of the lipid bilayer and along the normal (z) coordinate. For each window, 10 μs long simulations were performed. We should state, however, that MARTINI based simulations lead to an effective speed up of a factor of ~4 [], effectively giving a 40 μs time per window. PMFs were reconstructed using the weighted histogram [] approach and convergen […]

Want to access the full list of citations?
MARTINI institution(s)
Groningen Biomolecular Sciences and Biotechnology Institute & Zernike Institute for AdVanced Materials, Department of Biophysical Chemistry, University of Groningen, Groningen, The Netherlands; Zernike Institute for Advanced Materials, Department of Applied Physics, University of Groningen, Groningen, The Netherlands; Department of Biological Sciences, University of Calgary, Calgary, AB, Canada
MARTINI funding source(s)
Supported by the Netherlands Organisation for Scientific Research (NWO), an AHFMR Senior Scholar and CIHR New Investigator, and by NSERC.

MARTINI reviews

star_border star_border star_border star_border star_border
star star star star star

Be the first to review MARTINI