Abstract
Small heat shock proteins are present in nearly every form of life. However, despite their ubiquity, there are many questions about the structure of sHSPs. It is known that they can take a monomeric or an oligomeric form, and they have chaperone-like properties, meaning they help protect and fold other proteins. The aggregation and separation of these oligomers are reversible and controlled by environmental factors such as temperature and pH, but there are questions about the specifics of this process. I am growing up, purifying, and labeling sHSP so I can look into these questions using fluorescence correlation spectroscopy.
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Using FCS to Explore Agglomeration States of Small Heat Shock Proteins
Small heat shock proteins are present in nearly every form of life. However, despite their ubiquity, there are many questions about the structure of sHSPs. It is known that they can take a monomeric or an oligomeric form, and they have chaperone-like properties, meaning they help protect and fold other proteins. The aggregation and separation of these oligomers are reversible and controlled by environmental factors such as temperature and pH, but there are questions about the specifics of this process. I am growing up, purifying, and labeling sHSP so I can look into these questions using fluorescence correlation spectroscopy.