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MemDis: Predicting Disordered Regions in Transmembrane Proteins.
Dobson, Laszlo; Tusnády, Gábor E.
  • Dobson L; Institute of Enzymology, Research Centre for Natural Sciences, Magyar Tudósok Körútja 2, 1117 Budapest, Hungary.
  • Tusnády GE; Institute of Enzymology, Research Centre for Natural Sciences, Magyar Tudósok Körútja 2, 1117 Budapest, Hungary.
Int J Mol Sci ; 22(22)2021 Nov 12.
Article in English | MEDLINE | ID: covidwho-1534086
ABSTRACT
Transmembrane proteins (TMPs) play important roles in cells, ranging from transport processes and cell adhesion to communication. Many of these functions are mediated by intrinsically disordered regions (IDRs), flexible protein segments without a well-defined structure. Although a variety of prediction methods are available for predicting IDRs, their accuracy is very limited on TMPs due to their special physico-chemical properties. We prepared a dataset containing membrane proteins exclusively, using X-ray crystallography data. MemDis is a novel prediction method, utilizing convolutional neural network and long short-term memory networks for predicting disordered regions in TMPs. In addition to attributes commonly used in IDR predictors, we defined several TMP specific features to enhance the accuracy of our method further. MemDis achieved the highest prediction accuracy on TMP-specific dataset among other popular IDR prediction methods.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Neural Networks, Computer / Computational Biology / Intrinsically Disordered Proteins / Membrane Proteins Type of study: Prognostic study / Reviews Language: English Year: 2021 Document Type: Article Affiliation country: Ijms222212270

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Neural Networks, Computer / Computational Biology / Intrinsically Disordered Proteins / Membrane Proteins Type of study: Prognostic study / Reviews Language: English Year: 2021 Document Type: Article Affiliation country: Ijms222212270