High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility.

Amin, Nader T; Wallis, A Katrine; Wells, Stephen A; Rowe, Michelle L; Williamson, Richard A; Howard, Mark J; Freedman, Robert B

Amin, Nader T; Wallis, A Katrine; Wells, Stephen A; Rowe, Michelle L; Williamson, Richard A; Howard, Mark J; Freedman, Robert B.

Affiliation

Amin NT; School of Life Sciences, University of Warwick, Coventry CV4 7AL, UK.

Biochem J ; 450(2): 321-32, 2013 Mar 01.

Article in En | MEDLINE | ID: mdl-23234573

Subject(s)

Endoplasmic Reticulum/metabolism; Nuclear Magnetic Resonance, Biomolecular/methods; Protein Disulfide-Isomerases/chemistry; Binding Sites; Heat-Shock Proteins/chemistry; Heat-Shock Proteins/metabolism; Humans; Models, Molecular; Protein Disulfide-Isomerases/metabolism; Protein Folding; Protein Structure, Tertiary; X-Ray Diffraction

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Disulfide-Isomerases / Nuclear Magnetic Resonance, Biomolecular / Endoplasmic Reticulum Type of study: Prognostic_studies Limits: Humans Language: En Journal: Biochem J Year: 2013 Type: Article Affiliation country: United kingdom

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