Evidence map›Paper›PMID 34143353›Full record

ArticleInterdisciplinary sciences, computational life sciences2021

Sequence-Based Prediction of Transmembrane Protein Crystallization Propensity.

Qizhi Zhu, Lihua Wang, Ruyu Dai, Wei Zhang, Wending Tang, Yannan Bin, Zeliang Wang, Junfeng Xia

Abstract read
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In one paragraph

Article in Interdisciplinary sciences, computational life sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 57% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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

8 authors at 2 institutions in 1 country.

Qizhi Zhu *School of Information Engineering, Huangshan University, Huangshan, 245041, China.
Lihua Wang *School of Information Engineering, Huangshan University, Huangshan, 245041, China.
Ruyu DaiInstitutes of Physical Science and Information Technology, Anhui University, Hefei, 230601, China.
Wei ZhangInstitutes of Physical Science and Information Technology, Anhui University, Hefei, 230601, China.
Wending TangInstitutes of Physical Science and Information Technology, Anhui University, Hefei, 230601, China.
Yannan BinInstitutes of Physical Science and Information Technology, Anhui University, Hefei, 230601, China.
Zeliang WangSchool of Information Engineering, Huangshan University, Huangshan, 245041, China. mountwzl@hsu.edu.cn.ORCID http://orcid.org/0000-0001-5382-4300
Junfeng XiaInstitutes of Physical Science and Information Technology, Anhui University, Hefei, 230601, China. jfxia@ahu.edu.cn.
Anhui University · CNHuangshan University · CN

Funding

Anhui Provincial Outstanding Young Talent Support Plan gxyq2018083National Natural Science Foundation of China 11835014National Natural Science Foundation of China 62072003National Natural Science Foundation of China U19A2064
6 · The paper itself

Abstract

Transmembrane proteins play a vital role in cell life activities. There are several techniques to determine transmembrane protein structures and X-ray crystallography is the primary methodology. However, due to the special properties of transmembrane proteins, it is still hard to determine their structures by X-ray crystallography technique. To reduce experimental consumption and improve experimental efficiency, it is of great significance to develop computational methods for predicting the crystallization propensity of transmembrane proteins. In this work, we proposed a sequence-based machine learning method, namely Prediction of TransMembrane protein Crystallization propensity (PTMC), to predict the propensity of transmembrane protein crystallization. First, we obtained several general sequence features and the specific encoded features of relative solvent accessibility and hydrophobicity. Second, feature selection was employed to filter out redundant and irrelevant features, and the optimal feature subset is composed of hydrophobicity, amino acid composition and relative solvent accessibility. Finally, we chose extreme gradient boosting by comparing with other several machine learning methods. Comparative results on the independent test set indicate that PTMC outperforms state-of-the-art sequence-based methods in terms of sensitivity, specificity, accuracy, Matthew's Correlation Coefficient (MCC) and Area Under the receiver operating characteristic Curve (AUC). In comparison with two competitors, Bcrystal and TMCrys, PTMC achieves an improvement by 0.132 and 0.179 for sensitivity, 0.014 and 0.127 for specificity, 0.037 and 0.192 for accuracy, 0.128 and 0.362 for MCC, and 0.027 and 0.125 for AUC, respectively.

Indexed as

Computational BiologyMembrane ProteinsCrystallizationCrystallography, X-RayHydrophobic and Hydrophilic InteractionsMembrane ProteinsCrystallization propensityMachine learningProtein sequence featureTransmembrane protein

Identifiers

PMID34143353
OpenAlexW3169176548

What OpenQuestion holds

Textmetadata
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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.