کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1977942 | 1539300 | 2007 | 14 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Reactive cysteine in proteins: Protein folding, antioxidant defense, redox signaling and more
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Cysteine plays structural roles in proteins and can also participate in electron transfer reactions, when some structural folds provide appropriated environments for stabilization of its sulfhydryl group in the anionic form, called thiolate (RS−). In contrast, sulfhydryl group of free cysteine has a relatively high pKa (8,5) and as a consequence is relatively inert for redox reaction in physiological conditions. Thiolate is considerable more powerful as nucleophilic agent than its protonated form, therefore, reactive cysteine are present mainly in its anionic form in proteins. In this review, we describe several processes in which reactive cysteine in proteins take part, showing a high degree of redox chemistry versatility.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology - Volume 146, Issues 1–2, July–August 2007, Pages 180–193
Journal: Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology - Volume 146, Issues 1–2, July–August 2007, Pages 180–193
نویسندگان
Luis Eduardo Soares Netto, Marcos Antonio de Oliveira, Gisele Monteiro, Ana Paula Dias Demasi, José Renato Rosa Cussiol, Karen Fulan Discola, Marilene Demasi, Gustavo Monteiro Silva, Simone Vidigal Alves, Victor Genu Faria, Bruno Brasil Horta,