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The structural transformation comparison of the human Prion protein mutants V176G, E196A, and I215V by using molecular dynamics simulation

2021-03-03

Abstract excerpt

<title>Abstract</title> <p>The point mutations in the gene coding of prion protein (PrP) originate human familial prion protein (HuPrP) diseases. Such diseases are caused by several amino acid mutations of HuPrP including V176G, I215V, and E196A located at the second, third native helix and in their loop, respectively. Determining the transition from cellular prion protein (PrPc) to pathogenic conformer (PrPSc) i...

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Literature Corpus work
e15ceb89-42d3-518e-8522-62c51d0a41b5
DOI
10.21203/rs.3.rs-256266/v1
Open publication

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