دورية أكاديمية
Misfolding and Amyloid Aggregation of Apomyoglobin
| العنوان: | Misfolding and Amyloid Aggregation of Apomyoglobin |
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| المؤلفون: | Gaetano Irace, Rosa Maritato, Clara Iannuzzi, Ivana Sirangelo |
| المصدر: | International Journal of Molecular Sciences, Vol 14, Iss 7, Pp 14287-14300 (2013) |
| بيانات النشر: | MDPI AG, 2013. |
| سنة النشر: | 2013 |
| المجموعة: | LCC:Biology (General) LCC:Chemistry |
| مصطلحات موضوعية: | apomyoglobin folding, apomyoglobin misfolding, amyloid aggregation, Biology (General), QH301-705.5, Chemistry, QD1-999 |
| الوصف: | Apomyoglobin is an excellent example of a monomeric all α-helical globular protein whose folding pathway has been extensively studied and well characterized. Structural perturbation induced by denaturants or high temperature as well as amino acid substitution have been described to induce misfolding and, in some cases, aggregation. In this article, we review the molecular mechanism of the aggregation process through which a misfolded form of a mutated apomyoglobin aggregates at physiological pH and room temperature forming an amyloid fibril. The results are compared with data showing that either amyloid or aggregate formation occurs under particular denaturing conditions or upon cleavage of the residues corresponding to the C-terminal helix of apomyoglobin. The results are discussed in terms of the sequence regions that are more important than others in determining the amyloid aggregation process. |
| نوع الوثيقة: | article |
| وصف الملف: | electronic resource |
| اللغة: | English |
| تدمد: | 14071428 1422-0067 |
| Relation: | http://www.mdpi.com/1422-0067/14/7/14287; https://doaj.org/toc/1422-0067 |
| DOI: | 10.3390/ijms140714287 |
| URL الوصول: | https://doaj.org/article/ec75f7664021431c83f365055413b435 |
| رقم الأكسشن: | edsdoj.75f7664021431c83f365055413b435 |
| قاعدة البيانات: | Directory of Open Access Journals |
Full Text Finder | تدمد: | 14071428 14220067 |
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| DOI: | 10.3390/ijms140714287 |