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. Author manuscript; available in PMC: 2013 Sep 13.
Published in final edited form as: J Mol Biol. 2012 Mar 3;419(0):89–101. doi: 10.1016/j.jmb.2012.02.043

Figure 3.

Figure 3

UV-CD spectra and tryptophan fluorescence emission spectra of wild-type and mutant OmpF. a) Comparison of UV-CD spectra between wild-type and mutant OmpF protein. Measurements were recorded for protein concentration of 0.2 mg/mL. An average of three scans at 50 nm/min was acquired with a bandwidth of 0.2 nm and a response time of 1 second using three independent protein preparations. Final CD spectrum was then corrected for background by subtraction of spectrum of protein-free samples recorded under the same conditions. Noisy data below 200 nm has been removed. b) Comparison of tryptophan fluorescence emission spectra of wild type and mutant OmpF proteins. Measurements were recorded using samples containing 0.2 mg/mL protein held in a 1 mm path length cuvette, with an excitation wavelength of 290 nm. All mutants and wild-type OmpF protein exhibit similar characteristics in UV-CD and tryptophan fluorescence emission spectra, given that mutants R100L/G19W and R100L/G135W have one more tryptophan than the wild type protein. Thus, secondary structure formation and environment of the tryptophan residues in wild-type and mutant OmpF proteins are similar.