Your browser doesn't support javascript.
loading
Molecular dynamics simulations of site point mutations in the TPR domain of cyclophilin 40 identify conformational states with distinct dynamic and enzymatic properties.
Gur, Mert; Blackburn, Elizabeth A; Ning, Jia; Narayan, Vikram; Ball, Kathryn L; Walkinshaw, Malcolm D; Erman, Burak.
Afiliação
  • Gur M; Department of Mechanical Engineering, Faculty of Mechanical Engineering, Istanbul Technical University (ITU), Suite 445 Inönü Caddesi, No. 65 Gümüssuyu, 34437 Beyoglu, Istanbul, Turkey.
  • Blackburn EA; Centre for Translational and Chemical Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3FF, United Kingdom.
  • Ning J; Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh EH4 2XU, United Kingdom.
  • Narayan V; Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh EH4 2XU, United Kingdom.
  • Ball KL; Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh EH4 2XU, United Kingdom.
  • Walkinshaw MD; Centre for Translational and Chemical Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3FF, United Kingdom.
  • Erman B; Department of Chemical and Biological Engineering, Koc University College of Engineering, Eng 146 Rumeli Feneri Yolu, 34450 Sariyer, Istanbul, Turkey.
J Chem Phys ; 148(14): 145101, 2018 Apr 14.
Article em En | MEDLINE | ID: mdl-29655319

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Mutação Puntual / Ciclofilinas Limite: Humans Idioma: En Revista: J Chem Phys Ano de publicação: 2018 Tipo de documento: Article País de afiliação: Turquia País de publicação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Mutação Puntual / Ciclofilinas Limite: Humans Idioma: En Revista: J Chem Phys Ano de publicação: 2018 Tipo de documento: Article País de afiliação: Turquia País de publicação: Estados Unidos