Misfolding of a Single Disulfide Bonded Globular Protein into a Low-Solubility Species Conformationally and Biophysically Distinct from the Native One.

Saotome, Tomonori; Yamazaki, Toshio; Kuroda, Yutaka

Saotome, Tomonori; Yamazaki, Toshio; Kuroda, Yutaka.

Affiliation

Saotome T; Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology (TUAT), Tokyo 184-8588, Japan.
Yamazaki T; NMR Facility, Division of Structural and Synthetic Biology, Center for Life Science Technologies, RIKEN, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama City, Kanagawa 230-0045, Japan.
Kuroda Y; Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology (TUAT), Tokyo 184-8588, Japan. ykuroda@cc.tuat.ac.jp.

Biomolecules ; 9(6)2019 06 25.

Article in En | MEDLINE | ID: mdl-31242697

Subject(s)

Disulfides/chemistry; Protein Folding; Viral Envelope Proteins/chemistry; Biophysical Phenomena; Chemical Precipitation; Protein Conformation; Solubility

Key words

Single domain globular protein; aggregation-prone species; protein misfolding; protein refolding; single disulfide bond

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Viral Envelope Proteins / Protein Folding / Disulfides Language: En Journal: Biomolecules Year: 2019 Document type: Article Affiliation country: Japan Country of publication: Switzerland

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