Slow spontaneous α-to-ß structural conversion in a non-denaturing neutral condition reveals the intrinsically disordered property of the disulfide-reduced recombinant mouse prion protein. | Prion;6(5): 489-97, 2012. | MEDLINE

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Slow spontaneous α-to-ß structural conversion in a non-denaturing neutral condition reveals the intrinsically disordered property of the disulfide-reduced recombinant mouse prion protein.

Sang, Jason C; Lee, Chung-Yu; Luh, Frederick Y; Huang, Ya-Wen; Chiang, Yun-Wei; Chen, Rita P-Y.

Affiliation

Sang JC; Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.

Prion ; 6(5): 489-97, 2012.

Article in En | MEDLINE | ID: mdl-22987112

Subject(s)

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Prions / Protein Folding / Disulfides Limits: Animals Language: En Journal: Prion Journal subject: BIOQUIMICA Year: 2012 Document type: Article Affiliation country: Country of publication:

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Prions / Protein Folding / Disulfides Limits: Animals Language: En Journal: Prion Journal subject: BIOQUIMICA Year: 2012 Document type: Article Affiliation country: Country of publication: