Abstract:
:Conversion of the rod-like tobacco mosaic virus (TMV) virions into "ball-like particles" by thermal denaturation at 90-98 °C had been described by R.G. Hart in 1956. We have reported recently that spherical particles (SPs) generated by thermal denaturation of TMV at 94-98 °C were highly stable, RNA-free, and water-insoluble. The SPs were uniform in shape but varied widely in size (53-800 nm), which depended on the virus concentration. Here, we describe some structural characteristics of SPs using circular dichroism, fluorescence spectroscopy, and Raman spectroscopy. It was found that the structure of SPs protein differs strongly from that of the native TMV and is characterized by coat protein subunits transition from mainly (about 50%) α-helical structure to a structure with low content of α-helices and a significant fraction of β-sheets. The SPs demonstrate strong reaction with thioflavin T suggesting the formation of amyloid-like structures.
journal_name
J Biomol Struct Dynjournal_title
Journal of biomolecular structure & dynamicsauthors
Dobrov EN,Nikitin NA,Trifonova EA,Parshina EY,Makarov VV,Maksimov GV,Karpova OV,Atabekov JGdoi
10.1080/07391102.2013.788983subject
Has Abstractpub_date
2014-01-01 00:00:00pages
701-8issue
5eissn
0739-1102issn
1538-0254journal_volume
32pub_type
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