Hsp70: Difference between revisions
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==Structure of Hsp70== | ==Structure of Hsp70== | ||
<StructureSection load=' | <StructureSection load='5aqh<scene name='81/813405/Main_screen/3'></scene>' size='340' side='right';' scene=''> | ||
Here is a better first view of the molecule <scene name='81/813405/Main_screen/3'>here</scene>. | |||
'''Overview''' | '''Overview''' | ||
Chaperon proteins are important to almost all organisms. Their function is to assist in the folding of newly translated proteins unable to fold on their own and even refold proteins that have become nonfunctional due to some type of misfolding. Misfolding can be caused by several different types of stressors such as high temperature, starvation, inflammation, water deprivation, or nitrogen deficiency. Heat shock proteins, primarily the Hsp70 family, partially bind to the protein’s exposed hydrophobic surfaces, to promote protein refolding and prevent interactions that might lead to aggregation <ref>Sharma, D., & Masison, D. (2009). Hsp70 Structure, Function, Regulation and Influence on Yeast Prions. Protein & Peptide Letters, 16(6), 571-581. doi:10.2174/092986609788490230</ref>. | Chaperon proteins are important to almost all organisms. Their function is to assist in the folding of newly translated proteins unable to fold on their own and even refold proteins that have become nonfunctional due to some type of misfolding. Misfolding can be caused by several different types of stressors such as high temperature, starvation, inflammation, water deprivation, or nitrogen deficiency. Heat shock proteins, primarily the Hsp70 family, partially bind to the protein’s exposed hydrophobic surfaces, to promote protein refolding and prevent interactions that might lead to aggregation <ref>Sharma, D., & Masison, D. (2009). Hsp70 Structure, Function, Regulation and Influence on Yeast Prions. Protein & Peptide Letters, 16(6), 571-581. doi:10.2174/092986609788490230</ref>. | ||