Protein Misfolding Studies on Human Semenogelin-1 and Serum Albumin Proteins

Sharma, Neetu (2016) Protein Misfolding Studies on Human Semenogelin-1 and Serum Albumin Proteins. PhD thesis, Indian Institute of Technology Hyderabad.

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Proper folding of proteins into native structure is essential for their biological activity. Proteins achieve native state with the help of several cellular regulatory mechanismsassisted by molecular chaperones. Alteration in these regulatory mechanisms can lead to protein misfolding. Also failure to dispose of the misfolded protein load causes accumulation of misfolded proteins and toxicity. The accumulated protein in some cases may self-assemble into stable, β-sheet rich oligomers and aggregates known as amyloid fibrils. Amyloid aggregation has been implicated to cause several diseases such as Alzheimer’s, Parkinson’s and renal amyloidosis etc.

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IITH Creators:
IITH CreatorsORCiD
Item Type: Thesis (PhD)
Uncontrolled Keywords: Senile seminal vesicle amyloidosis, Human serum albumin, Dynamic light scattering, TD525
Subjects: Others > Biotechnology
Divisions: Department of Biotechnology
Depositing User: Library Staff
Date Deposited: 13 May 2016 11:05
Last Modified: 22 May 2019 05:34
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