Miles, Andrew J., Wien, Frank, Lees, Jonathan G., Rodger, Alison and Wallace, Bonnie Ann. (2003) Calibration and standardisation of synchrotron radiation circular dichroism and conventional circular dichroism spectrophotometers. Spectroscopy, Vol.17 (No.4). pp. 653-661. ISSN 1875-922X

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Abstract

Synchrotron radiation circular dichroism (SRCD) is an emerging technique in structural biology with particular value in protein secondary structure analyses since it permits the collection of data down to much lower wavelengths than conventional circular dichroism (cCD) instruments. Reference database spectra collected on different SRCD instruments in the future as well as current reference datasets derived from cCD spectra must be compatible. Therefore there is a need for standardization of calibration methods to ensure quality control. In this study, magnitude and optical rotation measurements on four cCD and three SRCD instruments were compared at 192.5, 219, 290 and 490 nm. At high wavelengths, all gave comparable results, however, at the lower wavelengths, some variations were observable. The consequences of these differences on the spectrum, and the calculated secondary secondary structure, of a representative protein (myoglobin) are demonstrated. A normalisation method is proposed for standardising spectra obtained on any CD instrument, conventional or SR-based, with respect to existing and future databases.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry
Divisions:	Faculty of Science > Chemistry
Library of Congress Subject Headings (LCSH):	Synchrotron radiation, Circular dichroism, Spectrophotometer -- Calibration
Journal or Publication Title:	Spectroscopy
Publisher:	I O S Press
ISSN:	1875-922X
Date:	2003
Volume:	Vol.17
Number:	No.4
Page Range:	pp. 653-661
Status:	Peer Reviewed
Access rights to Published version:	Restricted or Subscription Access
Funder:	Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), GlaxoSmithKline, Medical Research Council (Great Britain) (MRC)
Grant number:	B13586 (BBSRC), B14225 (BBSRC)
References:	[1] J.C. Sutherland, E.J. Desmond and P.Z. Takacs. Versatile spectrometer for experiments using synchrotron radiation at wavelengths greater than 100 nm. Nucl. Instr. Meth. 172 (1980),195-199. [2] P.A. Snyder and E.M.Rowe. The first use of synchrotron radiation for vacuum ultraviolet circular dichroism measurements. Nucl. Instr. Meth. 172 (1980), 345-349. [3] B.A. Wallace, F. Wien, A.J. Miles, J.G. Lees, P. Evans, S.V. Hoffman, G.J. Wistow and C. Slingsby. Biomedical applications of synchrotron radiation circular dichroism spectroscopy: Identification of mutant proteins associated with disease and development of a reference database for fold motifs, J. Chem. Soc. (2003), in press. [4] B.A. Wallace and R.W. Janes. Synchrotron radiation circular dichroism spectroscopy of proteins: Secondary structure, fold recognition, and structural genomics. Curr. Opin. Chem. Biol. 5 (2001), 567-571. [5] B.A. Wallace. Synchrotron radiation circular dichroism spectroscopy as a tool for investigating protein structures. J. Synch. Rad. 7 (2000), 289-295. [6] B. A. Wallace. First International Workshop on SRCD Spectroscopy. Synchrotron Radiation News 15 (2002), 20-22. [7] Wallace, B.A. and Teeters, C.L. Differential absorption flattening optical effects are significant in the circular dichroism spectra of large membrane fragments. Biochemistry 26 (1987), 65-70. [8] A. Lobley, L. Whitmore and B.A. Wallace. DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 18 (2002), 211-212. [9] L. Whitmore, A. Miles, and B.A. Wallace, in preparation. [10] N. Sreerama, and R.W. Woody. Estimation of protein secondary structure from CD spectra: Comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set. Anal. Biochemistry 282 (2000), 252-260. [11] G.C. Chen and J.T. Yang, Two-point calibration of circular dichrometer with d-10- camphorsulfonic acid. Anal. Lett. 10 (1977), 1195-1207. [12] T. Takakuwa, T. Konno and H. Meguro. A new standard substance for calibration of circular dichroism: ammonium d-10-camphorsulfonate. Anal. Sci. 1 (1985), 215-218. [13] K. Tuzimura, T. Konno, H. Meguro, M. Hatano, T. Murakimi, K. Kashiwabara, K. Saito, Y. Kondo and T.M. Suzuki. A critical study of the measurement and calibration of circular dichroism. Anal. Biochem. 81 (1977), 167-174. [14] T. Konno, H. Meguro and K Tuzimura. D-Pantolactone as a circular dichroism (CD) calibration. Anal. Biochem. 67 (1975), 226-232. [15] A.J. McCaffery and S.F. Mason. The electronic spectra, optical rotatory power and absolute configuration of metal complexes: The dextro-tris (ethylenediamine)colbalt (III) ion. Mol. Phys. 6 (1963), 359-371. [16] T.M. Lowry, Optical Rotatory Power, Dover Publications, New York (1964), p 407. [17] J.P. Hennessey, Jr and W. C. Johnson, Jr. Experimental errors and their effect on analysing circular dichroism spectra of proteins. Anal. Biochem.125 (1982), 177-188. [18] I.H.M. Van Stokkum, H.J.W. Spoelder, M. Bloemendal, R.Van Grondelle and F.C.A. Groen. Estimation of protein secondary structure and error analysis from CD spectra. Anal. Biochemistry 191 (1990), 110-118. [19] D. Mao, E. Wachter, and B.A.Wallace. Folding of the H+-ATPase proteolipid in phospholipid vesicles. Biochemistry 21(1982), 4960-4968. [20] P.H. Schippers and H.P.J.M. Dekkers. Direct determination of absolute circular dichroism data and calibration of commercial instruments. Anal. Chem. 53 (1981), 778- 782. [21] W.C. Johnson, Jr. Circular Dichroism Instrumentation. in: Circular Dichroism and the Conformational Analysis of Biomolecules,1996, Plenum Press, New York, p635-652. [22] S.Y. Venyaminov and J.T. Yang. Determination of Protein Secondary Structure. in: Circular Dichroism and the Conformational Analysis of Biomolecules,1996, Plenum Press, New York, p69-107. [23] B.A. Wallace, J. Lees, A.J.W. Orry, A. Lobley and R.W. Janes, R.W. Analyses of Circular Dichroism Spectra of Membrane Proteins. Protein Science 12 (2003), 875-884. [24] J. Lees and B.A. Wallace, Synchrotron radiation circular dichroism and conventional circular dichroism spectroscopy: A comparison. Spectroscopy 16 (2002), 121-125.
URI:	http://wrap.warwick.ac.uk/id/eprint/37553

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