Kerstin Nordstrand

Structure, dynamics and electrostatics of the active site of glutaredoxin 3 from Escherichia coli: comparison with functionally related proteins.

K. Berndt, N. Foloppe, L. Nilsson, 2001, Journal of molecular biology.

Direct NMR observation of the Cys‐14 thiol proton of reduced Escherichia coli glutaredoxin‐3 supports the presence of an active site thiol‐thiolate hydrogen bond

K. Berndt, G. Otting, A. Holmgren, 1999, FEBS letters.

NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism.

K. Berndt, G. Otting, A. Holmgren, 1999, Journal of molecular biology.

Glutaredoxin-3 from Escherichia coli

K. Berndt, H. Jörnvall, T. Bergman, 1996, The Journal of Biological Chemistry.

NMR structure of oxidized glutaredoxin 3 from Escherichia coli.

K. Berndt, G. Otting, A. Holmgren, 2000, Journal of molecular biology.

Updated Swedish advice on reducing the risk of sudden infant death syndrome

H. Lagercrantz, G. Wennergren, A. Berlin, 2015, Acta paediatrica.

Effect of urea on peptide conformation in water: molecular dynamics and experimental characterization.

K. Berndt, L. Nilsson, Ana Caballero-Herrera, 2005, Biophysical journal.