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J. Biochem, 2004, Vol. 135, No. 3 405-411
© 2004 The Japanese Biochemical Society

BIOCHEMISTRY

Secondary-Structure Analysis of Proteins by Vacuum-Ultraviolet Circular Dichroism Spectroscopy

Koichi Matsuo1, Ryuta Yonehara1 and Kunihiko Gekko1,2,*

1 Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, Higashi-Hiroshima 739-8526; and 2 Hiroshima Synchrotron Radiation Center, Hiroshima University, Higashi-Hiroshima 739-8526

The vacuum ultraviolet circular dichroism (VUVCD) spectra of 15 globular proteins (myoglobin, hemoglobin, human serum albumin, cytochrome c, peroxidase, {alpha}-lactalbumin, lysozyme, ovalbumin, ribonuclease A, ß-lactoglobulin, pepsin, trypsinogen, {alpha}-chymotrypsinogen, soybean trypsin inhibitor, and concanavalin A) were measured in aqueous solutions at 25°C in the wavelength region from 260 to 160 nm under a high vacuum, using a synchrotron-radiation VUVCD spectrophotometer. The VUVCD spectra below 190 nm revealed some characteristic bands corresponding to different secondary structures. The contents of {alpha}-helices, ß-strands, turns, and unordered structures were estimated using the SELCON3 program with VUVCD spectra data on the 15 proteins. Prediction of the secondary-structure contents was greatly improved by extending the circular dichroism spectra to 165 nm. The numbers of {alpha}-helix and ß-strand segments calculated from the distorted {alpha}-helix and ß-strand contents did not differ greatly from those obtained from X-ray crystal structures. These results demonstrate that synchrotron-radiation VUVCD spectroscopy is a powerful tool for analyzing the secondary structures of proteins.

* To whom correspondence should be addressed. E-mail: gekko{at}sci.hiroshima-u.ac.jp


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