Academic Journal

Conformational Effects of Serine Phosphorylation in Phospholamban Peptides

التفاصيل البيبلوغرافية
العنوان: Conformational Effects of Serine Phosphorylation in Phospholamban Peptides
المؤلفون: Quirk, Philip G., Patchell, Valerie B., Colyer, John, Drago, Guido A., Gao, Yuan
المصدر: European Journal of Biochemistry ; volume 236, issue 1, page 85-91 ; ISSN 0014-2956 1432-1033
بيانات النشر: Wiley
سنة النشر: 1996
المجموعة: Wiley Online Library (Open Access Articles via Crossref)
الوصف: We have employed one‐ and two‐dimensional 1 H‐NMR spectroscopy to study the effects of serine phosphorylation on peptide conformations, using cardiac phospholamban as a model system. The nonphosphorylated phospholamban 1–20 peptide has few restraints on the conformations available to it in aqueous solution. Phosphorylation at Ser16 results in greater constraints being placed on the region encompassing Arg14–Thr17, particularly at neutral pH when the phosphate group is in the di‐anionic form. These conformational restrictions arise from specific interactions between the side‐chain of Arg14 and the phosphate group. While substitution of phosphothreonine at position 16 causes generally similar effects to phosphoserine, aspartic acid has little effect. The results are compared with phosphorylation effects in other systems, including cardiac troponin I.
نوع الوثيقة: article in journal/newspaper
اللغة: English
DOI: 10.1111/j.1432-1033.1996.00085.x
الاتاحة: http://dx.doi.org/10.1111/j.1432-1033.1996.00085.x
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رقم الانضمام: edsbas.95ACFE49
قاعدة البيانات: BASE
الوصف
DOI:10.1111/j.1432-1033.1996.00085.x