M. Gür Et Al. , "Molecular dynamics simulations of site point mutations in the TPR domain of cyclophilin 40 identify conformational states with distinct dynamic and enzymatic properties," JOURNAL OF CHEMICAL PHYSICS , vol.148, no.14, 2018
Gür, M. Et Al. 2018. Molecular dynamics simulations of site point mutations in the TPR domain of cyclophilin 40 identify conformational states with distinct dynamic and enzymatic properties. JOURNAL OF CHEMICAL PHYSICS , vol.148, no.14 .
Gür, M., Blackburn, E. A., Ning, J., Narayan, V., Ball, K. L., Walkinshaw, M. D., ... Erman, B.(2018). Molecular dynamics simulations of site point mutations in the TPR domain of cyclophilin 40 identify conformational states with distinct dynamic and enzymatic properties. JOURNAL OF CHEMICAL PHYSICS , vol.148, no.14.
Gür, Mert Et Al. "Molecular dynamics simulations of site point mutations in the TPR domain of cyclophilin 40 identify conformational states with distinct dynamic and enzymatic properties," JOURNAL OF CHEMICAL PHYSICS , vol.148, no.14, 2018
Gür, Mert Et Al. "Molecular dynamics simulations of site point mutations in the TPR domain of cyclophilin 40 identify conformational states with distinct dynamic and enzymatic properties." JOURNAL OF CHEMICAL PHYSICS , vol.148, no.14, 2018
Gür, M. Et Al. (2018) . "Molecular dynamics simulations of site point mutations in the TPR domain of cyclophilin 40 identify conformational states with distinct dynamic and enzymatic properties." JOURNAL OF CHEMICAL PHYSICS , vol.148, no.14.
@article{article, author={Mert Gür Et Al. }, title={Molecular dynamics simulations of site point mutations in the TPR domain of cyclophilin 40 identify conformational states with distinct dynamic and enzymatic properties}, journal={JOURNAL OF CHEMICAL PHYSICS}, year=2018}