Evidence map›Paper›PMID 18197968›Full record

ArticleBMC bioinformatics2008

Combining sequence-based prediction methods and circular dichroism and infrared spectroscopic data to improve protein secondary structure determinations.

Jonathan G Lees, Robert W Janes

Abstract read
In one paragraph

Article in BMC bioinformatics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Methods for Molecular Modelling of Protein Complexes.Methods in molecular biology (Clifton, N.J.) · 2021
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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.

Jonathan G LeesSchool of Biological and Chemical Sciences, Queen Mary, University of London, London E1 4NS, UK. lees@biochem.ucl.ac.uk
Robert W Janes

Funding

Biotechnology and Biological Sciences Research Council BB/F010362/1
6 · The paper itself

Abstract

backgroundA number of sequence-based methods exist for protein secondary structure prediction. Protein secondary structures can also be determined experimentally from circular dichroism, and infrared spectroscopic data using empirical analysis methods. It has been proposed that comparable accuracy can be obtained from sequence-based predictions as from these biophysical measurements. Here we have examined the secondary structure determination accuracies of sequence prediction methods with the empirically determined values from the spectroscopic data on datasets of proteins for which both crystal structures and spectroscopic data are available.

resultsIn this study we show that the sequence prediction methods have accuracies nearly comparable to those of spectroscopic methods. However, we also demonstrate that combining the spectroscopic and sequences techniques produces significant overall improvements in secondary structure determinations. In addition, combining the extra information content available from synchrotron radiation circular dichroism data with sequence methods also shows improvements.

conclusionCombining sequence prediction with experimentally determined spectroscopic methods for protein secondary structure content significantly enhances the accuracy of the overall results obtained.

Indexed as

AlgorithmsModels, ChemicalAmino Acid SequenceCircular DichroismComputer SimulationModels, MolecularMolecular Sequence DataPeptide MappingProteinsProtein Structure, SecondarySequence Analysis, ProteinSpectrophotometry, InfraredSystems IntegrationProteins

Identifiers

PMID18197968
PMCPMC2253515

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LicenceCC BY
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Registered trials

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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.