أعرض في EDS

Stability of intracellular influenza virus nucleocapsid protein oligomers

التفاصيل البيبلوغرافية
العنوان: Stability of intracellular influenza virus nucleocapsid protein oligomers
المؤلفون: Prokudina En, N. P. Semenova, Chumakov Vm
المصدر: Archives of Virology. 150:833-839
بيانات النشر: Springer Science and Business Media LLC, 2005.
سنة النشر: 2005
مصطلحات موضوعية: Protein Conformation, Detergents, Orthomyxoviridae, General Medicine, Hydrogen-Ion Concentration, Biology, medicine.disease_cause, biology.organism_classification, Virology, Oligomer, Hydrophobic effect, chemistry.chemical_compound, Protein structure, chemistry, Influenza A virus, Ionic strength, medicine, RNA, Viral, Thermodynamics, Salts, Chemical stability, Nucleocapsid, Intracellular
الوصف: Stability of A/Duck/Ukrainae/63 (H3N8) influenza virus intracellular NP oligomers was studied using reducing agents, denaturants, detergents, salts, various pH and a range of temperatures. The results obtained indicate that influenza virus NP oligomers are noncovalently stabilized, and NP subunits are not linked by disulfide bonds. NP oligomers are thermostable and SDS resistant. Urea and high ionic strength also do not dissociate avian influenza virus intracellular NP oligomers. However, NP oligomers are completely dissociated at pH < 5. The data obtained suggest that hydrophobic bonds together with the electrostatic interactions take part in the stabilization of compact conformation of influenza virus NP oligomers. It was also shown that intrachain disulfides revealed in nascent NPs are reduced in NP subunits of NP oligomers, and this probably contributes to the stability and compactness of the oligomers.
تدمد: 1432-8798
0304-8608
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0817fdf8d26e42231ffb1ac53e69fd3b
https://doi.org/10.1007/s00705-004-0425-5
حقوق: CLOSED
رقم الأكسشن: edsair.doi.dedup.....0817fdf8d26e42231ffb1ac53e69fd3b
قاعدة البيانات: OpenAIRE
الوصف
تدمد:14328798
03048608