Circular Dichroism and Fluorescence Spectroscopy of Cysteinyl-tRNA Synthetase from Halobacterium salinarum ssp. NRC-1 Demonstrates that Group I Cations Are Particularly Effective in Providing Structure and Stability to This Halophilic Protein.

MLA

Reed, Christopher J., et al. “Circular Dichroism and Fluorescence Spectroscopy of Cysteinyl-TRNA Synthetase from Halobacterium Salinarum Ssp. NRC-1 Demonstrates That Group I Cations Are Particularly Effective in Providing Structure and Stability to This Halophilic Protein.” PLoS ONE, vol. 9, no. 3, Mar. 2014, pp. 1–7. EBSCOhost, https://doi.org/10.1371/journal.pone.0089452.

APA

Reed, C. J., Bushnell, S., & Evilia, C. (2014). Circular Dichroism and Fluorescence Spectroscopy of Cysteinyl-tRNA Synthetase from Halobacterium salinarum ssp. NRC-1 Demonstrates that Group I Cations Are Particularly Effective in Providing Structure and Stability to This Halophilic Protein. PLoS ONE, 9(3), 1–7. https://doi.org/10.1371/journal.pone.0089452

Chicago

Reed, Christopher J., Sarah Bushnell, and Caryn Evilia. 2014. “Circular Dichroism and Fluorescence Spectroscopy of Cysteinyl-TRNA Synthetase from Halobacterium Salinarum Ssp. NRC-1 Demonstrates That Group I Cations Are Particularly Effective in Providing Structure and Stability to This Halophilic Protein.” PLoS ONE 9 (3): 1–7. doi:10.1371/journal.pone.0089452.