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. Author manuscript; available in PMC: 2012 May 12.
Published in final edited form as: J Phys Chem B. 2011 Mar 10;115(18):5665–5677. doi: 10.1021/jp112298y

Figure 6.

Figure 6

The open band coherence spectra of the ferric form of the L358P mutant. The pump/probe excitation wavelengths are 423 nm and 412 nm for camphor-free and camphor-bound proteins, respectively. The left panels show the oscillatory components (circles) and the LPSVD fits (solid red lines). The LPSVD components corresponding to the dominant modes ~39 cm−1 and their phases are also shown. The right panel shows the corresponding power spectrum amplitudes. The modes near 36 and 147 cm−1 dominate the camphor-free form, whereas in the camphor-bound form, the modes near 147 cm−1 have disappeared and the modes at 39 cm−1 and ~ 64 cm−1 dominate the spectrum.