DynaMine statistics

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Citations per year

Number of citations per year for the bioinformatics software tool DynaMine

Tool usage distribution map

This map represents all the scientific publications referring to DynaMine per scientific context
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DynaMine specifications


Unique identifier OMICS_19044
Name DynaMine
Interface Web user interface
Restrictions to use None
Input data An amino acid sequence.
Output data Some dynamics profile.
Programming languages Python
Computer skills Basic
Stability Stable
Maintained Yes


  • person_outline Elisa Cilia

Publications for DynaMine

DynaMine citations


Exploring the Sequence based Prediction of Folding Initiation Sites in Proteins

Sci Rep
PMCID: 5562875
PMID: 28821744
DOI: 10.1038/s41598-017-08366-3

[…] We used 5 kinds of macro-features computed from the protein sequence using various tools. First, we used DynaMine, to predict the backbone dynamics of each protein. After the prediction, we shifted the dynamics values within each sequence constraining their range between 0 and 1, analogously to Pancsa e […]


Predictions of Backbone Dynamics in Intrinsically Disordered Proteins Using De Novo Fragment Based Protein Structure Predictions

Sci Rep
PMCID: 5539115
PMID: 28765603
DOI: 10.1038/s41598-017-07156-1
call_split See protocol

[…] namics in IDPs and that our method significantly surpasses any other method producing comparable information. We also develop a machine learning-based consensus predictor, which uses FRAGFOLD-IDP and DynaMine order parameter predictions to improve protein backbone dynamics predictions even further. […]


Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP

Sci Rep
PMCID: 5498717
PMID: 28680062
DOI: 10.1038/s41598-017-04611-x

[…] (MoRF). C-terminal regions of β propensity are highly conserved and have a conspicuous enrichment of post-translational modification (PTMs) sites, suggesting functional regulation of this region. The DynaMine profile also shows peaks in this region (Supplementary Fig. , underlined), which together predispose this region for mediating interaction(s) probably not based on induced folding. […]


Identification of a Drug Targeting an Intrinsically Disordered Protein Involved in Pancreatic Adenocarcinoma

Sci Rep
PMCID: 5213423
PMID: 28054562
DOI: 10.1038/srep39732
call_split See protocol

[…] ethods, all based solely on the knowledge of the protein sequence (). Order probability values span from 0, representing a highly dynamic protein residue, to 1, indicating a complete local stability. DynaMine was used to predict the S2 order parameter (, black line) for backbone N-H groups, which gives an estimate of likelihood of the protein chain flexibility. Although no residue is found in a st […]


Is unphosphorylated Rex, as multifunctional protein of HTLV 1, a fully intrinsically disordered protein? An in silico study

PMCID: 5613702
PMID: 28955936
DOI: 10.1016/j.bbrep.2016.07.018

[…] te and Doolitle scales were used to determine amino acid hydrophobicity [330]. The average flexibility of Rex was calculated by Kyte and Doolitle scales at (http://web.expasy.org/protscale/) and also DynaMine server at (http://dynamine.ibsquare.be/) . Charge-hydropathy plot and CDF (Cumulative Distribution Function) analysis (both available at http://www.pondr.com/cgi-bin/PONDR/pondr.cgi). Use of […]


Conserved Sequence Preferences Contribute to Substrate Recognition by the Proteasome*

PMCID: 4938175
PMID: 27226608
DOI: 10.1074/jbc.M116.727578
call_split See protocol

[…] The physicochemical properties of 115 sequences were calculated using the following tools: helix propensity, Agadir (); backbone dynamics, DynaMine (, ); disorder propensity, IUPred (); fraction of aliphatic, acidic, basic, nonpolar, aromatic or polar residues: EMBOSS pepstats (); entropy, SEG (, ); flexibility, FLEXPLOT (); and hydropho […]

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DynaMine institution(s)
MLG, Computer Science Department, Universite Libre de Bruxelles (ULB), Brussels, Belgium; Interuniversity Institute of Bioinformatics in Brussels (IB2), ULB-VUB, Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels, Belgium; Department of Structural Biology, VIB, Brussels, Belgium; Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary; AI-Lab, Computer Science Department, Vrije Universiteit Brussel, Brussels, Belgium
DynaMine funding source(s)
Supported by Brussels Institute for Research and Innovation (Innoviris) [BB2B 2010-1-12]; Belgian Fonds de la Recherche Scientifique (F.R.S.-FNRS) [2.4606.11 and 1.B.05914F]; Research Foundation - Flanders (FWO) [Odysseus G.0029.12].

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