Secondary structures of narcissus mosaic virus coat protein

• Published in: Journal of general virology Vol. 72; no. 6; pp. 1479 - 1480
• Main Authors: Wilson, Herbert R, Tollin, Patrick, Sawyer, Lindsay, Robinson, David J, Price, Nicholas C, Kelly, Sharon M
• Format: Journal Article
• Language: English
• Published: Reading Soc General Microbiol 01.06.1991; Society for General Microbiology
• Subjects: Biological and medical sciences; C.D; Capsid - chemistry; capsid protein; Circular Dichroism; Fundamental and applied biological sciences. Psychology; Microbiology; Morphology, structure, chemical composition, physicochemical properties; Mosaic Viruses - analysis; narcissus mosaic virus; papaya ringspot virus; potato virus X; Protein Conformation; secondary structure; Spectrophotometry, Ultraviolet - methods; Virology; X-Ray Diffraction - methods; Virus; Proteins; Narcissus mosaic virus; Plant pathogen; Molecular structure; Potexvirus; Circular dichroism spectrometry; Helical structure; Capsid
• ISSN: 0022-1317; 1465-2099
• DOI: 10.1099/0022-1317-72-6-1479

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. and 4 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 -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. Received 14 December 1990; accepted 1 March 1991.