Abstract
1 Department of Biological and Molecular Sciences, University of Stirling, Stirling FK9 4LA, U.K.
2 Department of Applied Physics and Electronic and Manufacturing Engineering, University of Dundee, Dundee DD1 4HN, U.K.
3 Department of Biochemistry, University of Edinburgh, Hugh Robson Building, George Square, Edinburgh EH8 9XD, U.K.
and4 Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, U.K.
Circular dichroism (CD) measurements on the coat protein of narcissus mosaic virus particles show that the dominant secondary structure is the α-helix, with a 45 (±2)% content. The -sheet content is much lower at 5 (±3)%. Both values are essentially the same as those found in potato virus X coat protein. The CD results are used to assess the results of secondary structure prediction methods.