Domain V of m-calpain shows the potential to form an oblique-orientated α-helix, which may modulate the enzyme's activity via interactions with anionic lipid

MLA

Frederick Harris, et al. “Domain V of M-Calpain Shows the Potential to Form an Oblique-Orientated α-Helix, Which May Modulate the Enzyme’s Activity via Interactions with Anionic Lipid.” European Journal of Biochemistry, vol. 269, Oct. 2002, pp. 5414–22. EBSCOhost, https://doi.org/10.1046/j.1432-1033.2002.03225.x.

APA

Frederick Harris, David A. Phoenix, Sarah R. Dennison, Klaus Brandenburg, & Ulrich Seydel. (2002). Domain V of m-calpain shows the potential to form an oblique-orientated α-helix, which may modulate the enzyme’s activity via interactions with anionic lipid. European Journal of Biochemistry, 269, 5414–5422. https://doi.org/10.1046/j.1432-1033.2002.03225.x

Chicago

Frederick Harris, David A. Phoenix, Sarah R. Dennison, Klaus Brandenburg, and Ulrich Seydel. 2002. “Domain V of M-Calpain Shows the Potential to Form an Oblique-Orientated α-Helix, Which May Modulate the Enzyme’s Activity via Interactions with Anionic Lipid.” European Journal of Biochemistry 269 (October): 5414–22. doi:10.1046/j.1432-1033.2002.03225.x.