دورية أكاديمية
Three-helix bundle and SH3-type barrels: autonomously stable structural motifs in small and large proteins.
| العنوان: | Three-helix bundle and SH3-type barrels: autonomously stable structural motifs in small and large proteins. |
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| المؤلفون: | Nikolsky KS; Institute of Biomedical Chemistry, Biobanking Group, Moscow, Russia., Kulikova LI; Institute of Biomedical Chemistry, Biobanking Group, Moscow, Russia., Petrovskiy DV; Institute of Biomedical Chemistry, Biobanking Group, Moscow, Russia., Rudnev VR; Institute of Biomedical Chemistry, Biobanking Group, Moscow, Russia., Butkova TV; Institute of Biomedical Chemistry, Biobanking Group, Moscow, Russia., Malsagova KA; Institute of Biomedical Chemistry, Biobanking Group, Moscow, Russia., Kopylov AT; Institute of Biomedical Chemistry, Biobanking Group, Moscow, Russia., Kaysheva AL; Institute of Biomedical Chemistry, Biobanking Group, Moscow, Russia. |
| المصدر: | Journal of biomolecular structure & dynamics [J Biomol Struct Dyn] 2023 Aug 28, pp. 1-15. Date of Electronic Publication: 2023 Aug 28. |
| Publication Model: | Ahead of Print |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Taylor & Francis Country of Publication: England NLM ID: 8404176 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1538-0254 (Electronic) Linking ISSN: 07391102 NLM ISO Abbreviation: J Biomol Struct Dyn Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: June 2012- : Oxon, UK : Taylor & Francis Original Publication: Guilderland, NY : Adenine Press, [c1983- |
| مستخلص: | In this study, we investigated two variants of a three-helix bundle and SH3-type barrel, compact in space, present in small and large proteins of various living organisms. Using a neural graph network, proteins with three-helix bundle ( n = 1377) and SH3-type barrels ( n = 1914) spatial folds were selected. Molecular experiments were performed for small proteins with these folds, and motifs were studied autonomously outside the protein environment at 300, 340, and 370 K. A comparative analysis of the main parameters of the structures in the course of the experiment was performed, including gyration radius, area accessible to the solvent, number of hydrophobic and hydrogen bonds, and root-mean-square deviation of atomic positions (RMSD). We exhibited an autonomous stability of the studied folds outside the protein environment in an aquatic medium. We aimed to demonstrate the possibility of analyzing three-helix bundle and SH3-type barrels autonomously outside the protein globule, thereby reducing the computational time and increasing performance without significant loss of information.Communicated by Ramaswamy H. Sarma. |
| فهرسة مساهمة: | Keywords: SH3-type barrels; Three-helix bundle; autonomous motif; molecular dynamics; small proteins; structural motif stability |
| تواريخ الأحداث: | Date Created: 20230828 Latest Revision: 20230828 |
| رمز التحديث: | 20240829 |
| DOI: | 10.1080/07391102.2023.2250450 |
| PMID: | 37640007 |
| قاعدة البيانات: | MEDLINE |
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Full Text Finder | تدمد: | 1538-0254 |
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| DOI: | 10.1080/07391102.2023.2250450 |