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. Author manuscript; available in PMC: 2011 May 1.
Published in final edited form as: J Mol Cell Cardiol. 2009 Oct 23;48(5):1007–1013. doi: 10.1016/j.yjmcc.2009.10.011

Fig 2.

Fig 2

R1500P and R1500W mutations do not detectibly alter the secondary structure of LMM. Far-UV CD spectra of WT (black) and mutant (gray) LMM were obtained from 250 nm – 200 nm at 4 °C. WT LMM has nearly identical secondary structure profiles to R1500P and R1500W LMM. All proteins display canonical α-helical spectra with characteristic minima at 208 nm and 222 nm, and the calculated percentage of α-helix is similar for all three proteins.