Evidence map›Paper›PMID 17828612›Full record

ArticleJournal of molecular modeling2007

Statistical analysis of physical-chemical properties and prediction of protein-protein interfaces.

Surendra S Negi, Werner Braun

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular modeling, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
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

26 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Article
  3. Integrative modeling of guanylate binding protein dimers.Protein science : a publication of the Protein Society · 2023
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  18. Review
  19. Structural analysis of linear and conformational epitopes of allergens.Regulatory toxicology and pharmacology : RTP · 2009
    Review
  20. 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 at 1 institution in 1 country.

Surendra S NegiDepartment of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555-0857, USA.
Werner Braun
The University of Texas Medical Branch at Galveston · US

Funding

Computational tools for T- and B-cell epitope predictionR01AI064913 · NIAID · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI BRAUN, WERNER A · 2005 to 2010
$1.6M
Interacting motifs of alphavirus envelope proteins.R21AI055746 · NIAID · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI BRAUN, WERNER A · 2003 to 2004
$598k
NIAID NIH HHS R01 AI064913NIAID NIH HHS R21 AI055746
6 · The paper itself

Abstract

We have developed a fully automated method, InterProSurf, to predict interacting amino acid residues on protein surfaces of monomeric 3D structures. Potential interacting residues are predicted based on solvent accessible surface areas, a new scale for interface propensities, and a cluster algorithm to locate surface exposed areas with high interface propensities. Previous studies have shown the importance of hydrophobic residues and specific charge distribution as characteristics for interfaces. Here we show differences in interface and surface regions of all physical chemical properties of residues as represented by five quantitative descriptors. In the current study a set of 72 protein complexes with known 3D structures were analyzed to obtain interface propensities of residues, and to find differences in the distribution of five quantitative descriptors for amino acid residues. We also investigated spatial pair correlations of solvent accessible residues in interface and surface areas, and compared log-odds ratios for interface and surface areas. A new scoring method to predict potential functional sites on the protein surface was developed and tested for a new dataset of 21 protein complexes, which were not included in the original training dataset. Empirically we found that the algorithm achieves a good balance in the accuracy of precision and sensitivity by selecting the top eight highest scoring clusters as interface regions. The performance of the method is illustrated for a dimeric ATPase of the hyperthermophile, Methanococcus jannaschii, and the capsid protein of Human Hepatitis B virus. An automated version of the method can be accessed from our web server at http://curie.utmb.edu/prosurf.html.

Indexed as

Adenosine TriphosphatasesAlgorithmsArchaeal ProteinsAutomationDatabases, ProteinDimerizationMethanococcusModels, MolecularMolecular ConformationProteinsAdenosine TriphosphatasesArchaeal ProteinsProteins

Identifiers

PMID17828612
PMCPMC2628805
OpenAlexW1973581737

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.