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Vacuum‐ultraviolet circular dichroism analysis of biomolecules
Author(s) -
Gekko Kunihiko,
Matsuo Koichi
Publication year - 2006
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.20252
Subject(s) - chemistry , circular dichroism , biomolecule , glycosidic bond , hydroxymethyl , crystallography , chromophore , spectroscopy , chirality (physics) , ab initio , synchrotron radiation , globular protein , analytical chemistry (journal) , stereochemistry , photochemistry , organic chemistry , biochemistry , enzyme , physics , nambu–jona lasinio model , chiral symmetry breaking , quantum mechanics , quark
The vacuum‐ultraviolet circular dichroism (VUVCD) spectra of various amino acids, saccharides, and proteins were measured using a synchrotron‐radiation CD spectrophotometer at HiSOR/HSRC that is capable of measuring the CD spectra down to 140 nm in aqueous solution. L ‐Isomers of amino acids show two successive positive peaks at around 200 and 180 nm depending on the side chain. The ab initio assignment by time‐dependent density functional theory predicts that these peaks are attributed to n–π* and π–π* transitions of the carboxyl group, respectively. Most mono‐ and disaccharides exhibit characteristic peaks at around 170 nm, sensitively depending on the anomeric and axial/equatorial configurations of hydroxyl groups, trans‐gauche conformations of the hydroxymethyl group, and the type of glycosidic linkage. The VUVCD spectra of 31 globular proteins allow us to estimate more accurately the content and number of α‐helix and β‐strand segments by extending the short‐wavelength limit of the analytical program SELCON3 down to 160 nm. These results demonstrate that synchrotron‐radiation VUVCD spectroscopy is a useful tool for structure analyses of biomolecules in solution based on the higher energy transitions of chromophores. Chirality, 2006. © 2006 Wiley‐Liss, Inc.