In silico folding and aggregation study of human amylin, an amyloidosis protein
Abnormal self-assembly of proteins converting their native conformations into β-sheet rich fibrillar structures is the hallmark of several so called "misfolding diseases" including Type 2 Diabetes Mellitus (T2DM), Alzheimer's and Parkinson's diseases, etc. Human islet amyloid pol...
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| Format: | Theses and Dissertations |
| Language: | English |
| Published: |
2012
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| Online Access: | https://hdl.handle.net/10356/50957 |
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| Institution: | Nanyang Technological University |
| Language: | English |
| Summary: | Abnormal self-assembly of proteins converting their native conformations into β-sheet rich fibrillar structures is the hallmark of several so called "misfolding diseases" including Type 2 Diabetes Mellitus (T2DM), Alzheimer's and Parkinson's diseases, etc. Human islet amyloid polypeptide (hlAPP or amylin) is the major component of amyloid deposits found in the pancreas of 90% T2DM patients. Although extensive studies have been performed in the recent decades, detailed information about hIAPP aggregation and the related pathology remains missing. |
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