A reference dataset for circular dichroism spectroscopy tailored for the betagamma-crystallin lens proteins.
Circular dichroism (CD) spectroscopy is a powerful solution technique for the study of protein secondary structure. As hierarchical euclidean clustering analyses of high quality crystallin synchrotron radiation circular dichroism (SRCD) spectral data can be separated into structural groups based solely on spectral information, the technique can potentially be improved to more accurately determine secondary structures and monitor conformational changes in crystallins. Secondary structure estimates can be determined through use of reference datasets of circular dichroism spectra from proteins with determined crystal structures. As with any empirical method, the accuracies of the analyses are dependent upon how closely the reference dataset characteristics match those of the protein to be studied. To date, crystallin proteins have not been well analysed by CD because existing reference datasets do not contain good representations of their structural characteristics. This work describes a betagamma-crystallin specific reference dataset, CRYST175, which was created solely for the study of betagamma-crystallin secondary structures. Prediction accuracy was assessed for the new dataset using several deconvolution algorithms and it was found to substantially outperform existing more general reference datasets.
Evans
P
P
Department of Crystallography, Birkbeck College, University of London, Malet Street, London, WC1E 7HX, UK.
Bateman
O A
OA
Slingsby
C
C
Wallace
B A
BA
D000465:Algorithms; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism / Q000379:methods*; D016000:Cluster Analysis; D019295:Computational Biology / Q000379:methods; D003459:Crystallins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D030562:Databases, Protein; D006801:Humans; D017433:Protein Structure, Secondary; D012016:Reference Values
D003459:Crystallins