Prion Interaction with Normal Protein in Topological Changing Secondary Structure to Aggregation | Zendy

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Prion Interaction with Normal Protein in Topological Changing Secondary Structure to Aggregation

Author(s) -

Yao Yao

Publication year - 2020

Publication title -

advanced emergency medicine

Language(s) - English

Resource type - Journals

ISSN - 2315-456X

DOI - 10.18686/aem.v9i2.167

Subject(s) - protein secondary structure , helix (gastropod) , nucleic acid , infectivity , fibril , hydrogen bond , dna , chemistry , amyloid (mycology) , biophysics , beta sheet , protein structure , virus , crystallography , biology , virology , biochemistry , molecule , inorganic chemistry , ecology , organic chemistry , snail

Prion is a protein smaller than virus and it infects host in the absence of nucleic acid. The secondary structure of protein folds incorrectly from α-helices to β-sheets through breaking and re-formation of hydrogen bond. Structural analogy of α-helix and DNA double helix and comparing differences between α-helix and β-sheet show prion's infectivity and propagation. Aggregates of dimers and polymers generate β-amyloid fibril in Alzheimer's disease.

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