InterProSurf protocols

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InterProSurf specifications

Information


Unique identifier OMICS_08136
Name InterProSurf
Interface Web user interface
Restrictions to use None
Input data Macromolecular structure data
Input format PDB
Computer skills Basic
Stability Stable
Maintained Yes

Publication for InterProSurf

InterProSurf in pipeline

2014
PMCID: 3985705
PMID: 24433110
DOI: 10.1021/bi401525h

[…] and ha2 residues 76–110. the orientation of the r domain was calculated by the dyndomain server (http://fizz.cmp.uea.ac.uk/dyndom/)., the solvent accessible surface area (sasa) was analyzed by using interprosurf server (http://curie.utmb.edu/prosurf.html). the ha1–ha1 interface area was calculated by the formula sasa(three monomeric ha1) – sasa(trimeric ha1)., the cavity was found by the 3v […]


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InterProSurf in publications

 (11)
PMCID: 5498776
PMID: 28690376
DOI: 10.6026/97320630013122

[…] proteinprotein docking solutions []. the docked complexes based on their energy scores (kj/mole), a comparative analysis was carried out and visualized with the help of discovery studio 3.5., interprosurf was used for protein-protein interactions studies of the docked molecules, which investigated the role of hydrogen bond formation, hydrophobic residues and overall electrostatics […]

PMCID: 5133558
PMID: 27910934
DOI: 10.1038/srep38372

[…] docking complex with the pairwise shape complementarity, desolvation, and electrostatic energy methods. the interaction residues of the vimentin rod and denv-2 ediii proteins were predicted by the interprosurf software, and an interacting interface was analyzed by the pymol 1.7.3 software., how to cite this article: yang, j. et al. superficial vimentin mediates denv-2 infection of vascular […]

PMCID: 5056509
PMID: 27721441
DOI: 10.1038/srep34869

[…] to the internal residue arg35 next to the mutation phe34 → val. as a complementary approach, we analyzed each reference conformation with the web-tool protein-protein interaction predictor interprosurf to identify the hydrophobic solvent-accessible residues, prone to interact with other protein groups. we then represented the residues selected from both approaches (see ) and we grouped […]

PMCID: 4677168
PMID: 26697220
DOI: 10.1155/2015/978193

[…] accessibility (sa) that exceeded 1.0 å2 compared to that in the monomer formation. an amino acid residue was classified to be either interface class or noninterface. in this paper we used web server interprosurf available at website http://curie.utmb.edu/pdbcomplex.html to determine the interface residue of protein complexes from its pdb number. dset186 consists of 36219 residues of which 4241 […]

PMCID: 4662854
PMID: 26341627
DOI: 10.15252/embr.201540436

[…] by hydrophilic residues (namely d142, d166 and e171) (fig f). this surface and c‐terminus tail (174atlnnvktl182) were predicted as potential protein–protein interaction (ppi) interfaces by the interprosurf analysis (fig a and c) and the consensus protein–protein interaction site predictor (cons‐ppisp) server (fig b and c). in the crystals of t4 lysozyme‐mcu ntd and mcu ntd‐e, mcu ntds […]


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InterProSurf institution(s)
Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX, USA

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