دورية أكاديمية

Amide-π interactions in active centers of superoxide dismutase

التفاصيل البيبلوغرافية
العنوان: Amide-π interactions in active centers of superoxide dismutase
المؤلفون: Stojanović Srđan Đ., Petrović Zoran Z., Zlatović Mario V.
المصدر: Journal of the Serbian Chemical Society, Vol 86, Iss 9, Pp 781-793 (2021)
بيانات النشر: Serbian Chemical Society, 2021.
سنة النشر: 2021
المجموعة: LCC:Chemistry
مصطلحات موضوعية: catalytic site, distribution of distances, stabilization of the sod proteins, Chemistry, QD1-999
الوصف: In this work, the influence of amide–π interactions on stability and properties of superoxide dismutase (SOD) active centres was analysed. In the data set of 43 proteins, 5017 amide–π interactions were observed, and every active centre formed averagely about 117 interactions. Most of the interactions belonged to the backbone of proteins. The analysis of the geometry of the amide–π interactions revealed two preferred structures, parallel-displaced and T-shaped structure. The aim of this study was to investigate the energy contribution resulting the from amide–π interactions, which were in the lower range of strong hydrogen bonds. The conservation patterns in the present study indicate that more than half of the residues involved in these interactions are evolutionarily conserved. The stabilization centres for these proteins showed that all residues involved in amide–π interactions were of use in locating one or more of such centres. The results presented in this work can be very useful for the understanding of contribution of amide–π interaction to the stability of SOD active centres.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 0352-5139
1820-7421
Relation: https://doaj.org/toc/0352-5139; https://doaj.org/toc/1820-7421
DOI: 10.2298/JSC210321042S
URL الوصول: https://doaj.org/article/a3414e4322e34ecc9c9106feefaa4ac9
رقم الأكسشن: edsdoj.3414e4322e34ecc9c9106feefaa4ac9
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:03525139
18207421
DOI:10.2298/JSC210321042S