Evidence map›Paper›PMID 30954029›Full record

ArticleIranian biomedical journal2019

Physicochemical Position-Dependent Properties in the Protein Secondary Structures

Ehsan Saghapour, Mohammadreza Sehhati

Abstract read
In one paragraph

Article in Iranian biomedical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

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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.

Ehsan SaghapourDepartment of Bioelectronic and Biomedical Engineering, School of Advanced Technologies in Medicine, Isfahan University of Medical Sciences, Isfahan, Iran.
Mohammadreza SehhatiDepartment of Bioelectronic and Biomedical Engineering, School of Advanced Technologies in Medicine, Isfahan University of Medical Sciences, Isfahan, Iran.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: Establishing theories for designing arbitrary protein structures is complicated and depends on understanding the principles for protein folding, which is affected by applied features. Computer algorithms can reach high precision and stability in computationally designed enzymes and binders by applying informative features obtained from natural structures. Methods: In this study, a position-specific analysis of secondary structures (α-helix, β-strand, and tight turn) was performed to reveal novel features for protein structure prediction and protein design. Results: Our results showed that the secondary structures in the N-termini region tend to be more compact than C-termini. Decoying periodicity in length and distribution of amino acids in α-helices is deciphered using the curve-fitting methods. Compared with α-helix, β-strands do not show distinct periodicities in length. Also, significant differences in position-dependent distribution of physicochemical properties are shown in secondary structures. Conclusion: Position-specific propensities in our study underline valuable parameters that could be used by researchers in the field of structural biology, particularly protein design through site-directed mutagenesis.

Indexed as

Chemical PhenomenaAmino AcidsDatabases, ProteinPosition-Specific Scoring MatricesProteinsProtein Structure, SecondaryAmino AcidsProteinsAlgorithmsAmino acidsPhysicochemicalProtein structure

Identifiers

PMID30954029
PMCPMC6462287

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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.