Misfolding and Amyloid Aggregation of Apomyoglobin
| Autor: | Clara Iannuzzi, Gaetano Irace, Ivana Sirangelo, Rosa Maritato |
|---|---|
| Přispěvatelé: | Iannuzzi, Clara, Maritato, R, Irace, Gaetano, Sirangelo, Ivana |
| Rok vydání: | 2013 |
| Předmět: |
apomyoglobin folding
Amyloid Protein Folding amyloid aggregation Globular protein Protein aggregation Cleavage (embryo) Protein Aggregation Pathological Article apomyoglobin misfolding Protein Structure Secondary Catalysis lcsh:Chemistry Inorganic Chemistry Protein structure Animals Humans Physical and Theoretical Chemistry lcsh:QH301-705.5 Molecular Biology Spectroscopy chemistry.chemical_classification Myoglobin Organic Chemistry General Medicine Hydrogen-Ion Concentration Protein Structure Tertiary Computer Science Applications Folding (chemistry) lcsh:Biology (General) lcsh:QD1-999 chemistry Biochemistry Mutation Helix Protein folding Apoproteins |
| Zdroj: | International Journal of Molecular Sciences International Journal of Molecular Sciences, Vol 14, Iss 7, Pp 14287-14300 (2013) |
| ISSN: | 1422-0067 |
| DOI: | 10.3390/ijms140714287 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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