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Spectroscopy
Volume 19 (2005), Issue 1, Pages 43-51
http://dx.doi.org/10.1155/2005/263649

Calibration and standardisation of synchrotron radiation and conventional circular dichroism spectrometers. Part 2: Factors affecting magnitude and wavelength

Andrew J. Miles,1 Frank Wien,1 Jonathan G. Lees,1,3 and B.A. Wallace1,2

1Department of Crystallography, Birkbeck College, University of London, London WC1E 7HX, United Kingdom
2Centre for Protein and Membrane Structure and Dynamics, Daresbury Laboratory, Warrington WA4 4AD, United Kingdom
3School of Biological Sciences, Queen Mary, University of London, London E1 4NS, United Kingdom

Copyright © 2005 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Citations to this Article [31 citations]

The following is the list of published articles that have cited the current article.

  • Wien, and Wallace, “Calcium fluoride micro cells for synchrotron radiation circular dichroism spectroscopy,” Applied Spectroscopy, vol. 59, no. 9, pp. 1109–1113, 2005. View at Publisher · View at Google Scholar
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  • Wien, Miles, Lees, Vrønning Hoffmann, and Wallace, “VUV irradiation effects on proteins in high-flux synchrotron radiation circular dichroism spectroscopy,” Journal of Synchrotron Radiation, vol. 12, no. 4, pp. 517–523, 2005. View at Publisher · View at Google Scholar
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  • Jonathan G. Lees, Andrew J. Miles, Frank Wien, and B. A. Wallace, “A reference database for circular dichroism spectroscopy covering fold and secondary structure space,” Bioinformatics, vol. 22, no. 16, pp. 1955–1962, 2006. View at Publisher · View at Google Scholar
  • Tao Bo, and Janusz Pawliszyn, “Characterization of phospholipid–protein interactions by capillary isoelectric focusing with whole-column imaging detection,” Analytical Biochemistry, vol. 350, no. 1, pp. 91–98, 2006. View at Publisher · View at Google Scholar
  • Jonathan G. Lees, Andrew J. Miles, Robert W. Janes, and Wallace, “Novel methods for secondary structure determination using low wavelength (VUV) circular dichroism spectroscopic data,” BMC Bioinformatics, vol. 7, 2006. View at Publisher · View at Google Scholar
  • Andrew J. Miles, and B. A. Wallace, “Synchrotron radiation circular dichroism spectroscopy of proteins and applications in structural and functional genomics,” Chemical Society Reviews, vol. 35, no. 1, pp. 39, 2006. View at Publisher · View at Google Scholar
  • Lee Whitmore, and Wallace, “Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases,” Biopolymers, vol. 89, no. 5, pp. 392–400, 2008. View at Publisher · View at Google Scholar
  • Peter McPhie, “Concentration-independent estimation of protein secondary structure by circular dichroism: a comparison of methods,” Analytical Biochemistry, vol. 375, no. 2, pp. 379–381, 2008. View at Publisher · View at Google Scholar
  • Cedric Dicko, Matthew R. Hicks, Timothy R. Dafforn, Fritz Vollrath, Alison Rodger, and Søren V. Hoffmann, “Breaking the 200nm Limit for Routine Flow Linear Dichroism Measurements Using UV Synchrotron Radiation,” Biophysical Journal, vol. 95, no. 12, pp. 5974–5977, 2008. View at Publisher · View at Google Scholar
  • Jonathan G. Lees, and Robert W. Janes, “Combining sequence-based prediction methods and circular dichroism and infrared spectroscopic data to improve protein secondary structure determinations,” Bmc Bioinformatics, vol. 9, 2008. View at Publisher · View at Google Scholar
  • Masahito Tanaka, Kazutoshi Yagi-Watanabe, Fusae Kaneko, and Kazumichi Nakagawa, “Compact optical cell system for vacuum ultraviolet absorption and circular dichroism spectroscopy and its application to aqueous solution sample,” Chirality, vol. 20, no. 9, pp. 1023–1028, 2008. View at Publisher · View at Google Scholar
  • Masahito Tanaka, Kazutoshi Yagi-Watanabe, Fusae Kaneko, and Kazumichi Nakagawa, “Accurate and quick calibration method for polarization-modulation spectroscopy using an ac-modulated polarizing undulator,” Review of Scientific Instruments, vol. 79, no. 8, 2008. View at Publisher · View at Google Scholar
  • Wallace, “Protein characterisation by synchrotron radiation circular dichroism spectroscopy,” Quarterly Reviews of Biophysics, vol. 42, no. 4, pp. 317–370, 2009. View at Publisher · View at Google Scholar
  • Wallace, and Robert W. Janes, “Synchrotron radiation circular dichroism (SRCD) spectroscopy: An enhanced method for examining protein conformations and protein interactions,” Biochemical Society Transactions, vol. 38, no. 4, pp. 861–873, 2010. View at Publisher · View at Google Scholar
  • A. M. Powl, A. O. O'Reilly, A. J. Miles, and B. A. Wallace, “Synchrotron radiation circular dichroism spectroscopy-defined structure of the C-terminal domain of NaChBac and its role in channel assembly,” Proceedings of the National Academy of Sciences, vol. 107, no. 32, pp. 14064–14069, 2010. View at Publisher · View at Google Scholar
  • Jascindra Ravi, Frank Wien, Liqing Wu, Curtis W. Meuse, Alex E. Knight, Paulina D. Rakowska, Tommaso Garfagnini, Bruno Baron, Philippe Charlet, Christopher Jones, Stoyan Milev, Julie Desa Lorenz, and David Plusquellic, “International comparability in spectroscopic measurements of protein structure by circular dichroism: CCQM-P59.1,” Metrologia, vol. 47, no. 6, pp. 631–641, 2010. View at Publisher · View at Google Scholar
  • Ettore Castiglioni, Paolo Albertini, and Sergio Abbate, “Evaluation of instrumental errors built in circular dichroism spectrometers,” Chirality, vol. 22, no. 1E, pp. E142–E148, 2010. View at Publisher · View at Google Scholar
  • B.A. Wallace, Kunihiko Gekko, Søren Vrønning Hoffmann, Yi-Hung Lin, John C. Sutherland, Ye Tao, Frank Wien, and Robert W. Janes, “Synchrotron radiation circular dichroism (SRCD) spectroscopy: An emerging method in structural biology for examining protein conformations and protein interactions,” Nuclear Instruments and Methods in Physics Research Section A: Accelerators, Spectrometers, Detectors and Associated Equipment, vol. 649, no. 1, pp. 177–178, 2011. View at Publisher · View at Google Scholar
  • Ali Abdul-Gader, Andrew John Miles, and Wallace, “A reference dataset for the analyses of membrane protein secondary structures and transmembrane residuesusing circular dichroism spectroscopy,” Bioinformatics, vol. 27, no. 12, pp. 1630–1636, 2011. View at Publisher · View at Google Scholar
  • Robert W. Janes, A.J. Miles, B. Woollett, L. Whitmore, D. Klose, and B.A. Wallace, “Circular dichroism spectral data and metadata in the Protein Circular Dichroism Data Bank (PCDDB): A tutorial guide to accession and deposition,” Chirality, vol. 24, no. 9, pp. 751–763, 2012. View at Publisher · View at Google Scholar
  • D. P. Klose, B. A. Wallace, and R. W. Janes, “DichroMatch: a website for similarity searching of circular dichroism spectra,” Nucleic Acids Research, vol. 40, no. W1, pp. W547–W552, 2012. View at Publisher · View at Google Scholar
  • B. Woollett, L. Whitmore, R. W. Janes, and B. A. Wallace, “ValiDichro: a website for validating and quality control of protein circular dichroism spectra,” Nucleic Acids Research, 2013. View at Publisher · View at Google Scholar
  • F Wien, M Paternostre, F Gobeaux, F Artzner, and M Refregiers, “Calibration and quality assurance procedures at the far UV linear and circular dichroism experimental station DISCO,” Journal of Physics: Conference Series, vol. 425, no. 12, pp. 122014, 2013. View at Publisher · View at Google Scholar
  • Maurice G Cox, Jascindra Ravi, Paulina D Rakowska, and Alex E Knight, “Uncertainty in measurement of protein circular dichroism spectra,” Metrologia, vol. 51, no. 1, pp. 67–79, 2014. View at Publisher · View at Google Scholar
  • Dale L. Ang, Benjamin W. J. Harper, Leticia Cubo, Oscar Mendoza, Ramon Vilar, and Janice Aldrich-Wright, “Quadruplex DNA-Stabilising Dinuclear Platinum(II) Terpyridine Complexes with Flexible Linkers,” Chemistry - A European Journal, 2015. View at Publisher · View at Google Scholar
  • Xue-Ying Liu, Hong-Yan Zeng, Meng-Chen Liao, Bi Foua Claude Alain Gohi, and Bo Feng, “Determination of the kinetics and influence of the mercury ion on papain catalytic activity,” RSC Adv., vol. 5, no. 84, pp. 68906–68913, 2015. View at Publisher · View at Google Scholar
  • Sachin Mane, “Racemic drug resolution: a comprehensive guide,” Anal. Methods, 2016. View at Publisher · View at Google Scholar
  • A. J. Miles, and B. A. Wallace, “Circular dichroism spectroscopy of membrane proteins,” Chem. Soc. Rev., 2016. View at Publisher · View at Google Scholar