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![[Figure 3]](ig5018fig3mag.jpg)
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Figure 3
(a) Comparison of SRCD spectra of myoglobin in aqueous solution, recorded on UV-CD12 at ANKA and on CD12 at Daresbury [spectrum was taken from the protein circular dichroism data bank: PCDDBID CD0000047000 (Lees et al., 2006  )]; the dashed curve shows the HV applied on the PMT (ET 9406B) during the measurement at UV-CD12 and the vertical dotted line indicates the cut-off wavelength, which is typically reached at a HV of ∼400 V; data above this cut-off HV are not reliable. (b) Raw data of the myoglobin sample and H2O baseline spectra collected on UV-CD12; a 300 ms lock-in amplifier time constant and a 1.5 s dwell time have been used; the spectrum presented in (a) was averaged over the three raw spectra and the average of the three baseline spectra was subtracted and after Savitzky-Golay smoothening the ellipticities were converted to Δ∊ using the mean residue molar concentration of the protein and the cuvette path length. (c) 20 consecutive scans of human serum albumin, a protein that is highly sensitive to UV-radiation-induced denaturation; the first and last scan are black solid and dashed lines, respectively; no decrease of the signal magnitude is observed for all spectra, which proves the absence of any denaturation effects even at the conditions close to the maximum electron beam current of 160 mA used for this experiment. |
![[Figure 3]](ig5018fig3.jpg)
 | JOURNAL OF SYNCHROTRON RADIATION |
ISSN: 1600-5775
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