Orry A J, Janes R W, Sarra R, Hanlon M R, Wallace B A
Department of Crystallography, Birkbeck College, University of London, London WC1E 7HX, UK.
J Synchrotron Radiat. 2001 May 1;8(3):1027-9. doi: 10.1107/s0909049501004496.
Synchrotron radiation circular dichroism (SRCD) spectroscopy is an emerging technique for sensitive determination of protein secondary structures and for monitoring of conformational changes. An important issue for its adoption as a useful technique is whether the high-intensity low-wavelength vacuum ultraviolet radiation in the SRCD chemically damages proteins. In this paper, using horse myoglobin as a test sample, it is shown that extensive irradiation in the SRCD does not produce any change in the chemical nature of the protein as detected by either SDS gel electrophoresis or mass spectrometry. In addition, no changes in the protein secondary structure are detectable from the SRCD spectra after extensive exposure to the SRCD beam.
同步辐射圆二色光谱（SRCD）是一种新兴技术，用于灵敏地测定蛋白质二级结构并监测构象变化。将其作为一种实用技术采用时的一个重要问题是，SRCD中高强度的低波长真空紫外辐射是否会对蛋白质造成化学损伤。在本文中，以马肌红蛋白作为测试样品，结果表明，通过SDS凝胶电泳或质谱检测发现，SRCD中的长时间照射不会使蛋白质的化学性质发生任何变化。此外，在长时间暴露于SRCD光束后，从SRCD光谱中未检测到蛋白质二级结构的变化。
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