Academic Journal
Copyright © 2009 JMS The Role of Glu367 in the Quaternary Structure of Goose δ-crystallin
| العنوان: | Copyright © 2009 JMS The Role of Glu367 in the Quaternary Structure of Goose δ-crystallin |
|---|---|
| المؤلفون: | Chih-wei Huang, J Med Sci, Hwei-jen Lee |
| المساهمون: | The Pennsylvania State University CiteSeerX Archives |
| المصدر: | http://jms.ndmctsgh.edu.tw/fdarticlee/2906315.pdf. |
| سنة النشر: | 2009 |
| المجموعة: | CiteSeerX |
| مصطلحات موضوعية: | point |
| الوصف: | δ-Crystallin is a soluble structural protein that is recruited from argininosuccinate lyase through gene sharing to confer special refractive properties in avian eye lenses. The present study investigates the role of Glu367. This residue is located in the interface of the double dimer. Mutation in Glu367 caused no subtle changes in the conformation and stability of the secondary and tertiary structure as compared to wild-type protein. However, dissociated dimeric form was observed for E367A mutant protein. The dissociated dimers were unstable and prone to form protein aggregates. These results in-dicate that the interactions provided by E367 in the dimer-dimer interface of δ-crystallin are important for double dimer assembly. |
| نوع الوثيقة: | text |
| وصف الملف: | application/pdf |
| اللغة: | English |
| Relation: | http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.585.1358; http://jms.ndmctsgh.edu.tw/fdarticlee/2906315.pdf |
| الاتاحة: | http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.585.1358 http://jms.ndmctsgh.edu.tw/fdarticlee/2906315.pdf |
| Rights: | Metadata may be used without restrictions as long as the oai identifier remains attached to it. |
| رقم الانضمام: | edsbas.4DD09C1D |
| قاعدة البيانات: | BASE |
| الوصف غير متاح. |