1. Caspar Carboxylates: The Structural Basis of Tobamovirus Disassembly
Hong Wang, Antonio Planchart, Gerald Stubbs 
Biophysical Journal 
Volume 74, Issue 1, Pages (January 1998)
DOI: /S (98)
Copyright © 1998 The Biophysical Society Terms and Conditions

2. Figure 1
Ribbon drawings of two axially adjacent subunits from each of the five tobamoviruses TMV, U2, ORSV, CGMMV, and RMV. Potential axially interacting carboxylate side chains are shown. Note that in sequence alignments (Altschuh et al., 1987), Asp79 in ORSV aligns with Glu77 in TMV. To show the carboxylates clearly, the direction of view is reversed for CGMMV. The upper subunit is 16 subunits along the viral helix from the lower subunit, except in the case of CGMMV, where it is 17 subunits along the helix. The viral axis would be vertical and to the right of the figures, except in the case of CGMMV, where it would be to the left.
Biophysical Journal  , DOI: ( /S (98) )
Copyright © 1998 The Biophysical Society Terms and Conditions

3. Figure 2
Ribbon drawings of the inner loops of four subunits from each of the five tobamoviruses, viewed approximately from the center of the virus. Carboxylate side chains interact both laterally and axially, except in U2, but the nature of the interactions varies dramatically. Carboxylate side chains are shown.
Biophysical Journal  , DOI: ( /S (98) )
Copyright © 1998 The Biophysical Society Terms and Conditions

4. Figure 3
Electrostatic surface potentials of four subunits of each of the five tobamoviruses, viewed approximately from the center of the virus. Negatively charged areas are shown singly cross-hatched; positively charged regions are doubly cross-hatched.
Biophysical Journal  , DOI: ( /S (98) )
Copyright © 1998 The Biophysical Society Terms and Conditions

5. Figure 4
Electrostatic surface potentials of two subunits of TMV, positioned so that the surfaces that will face each other in the virus both face the reader in the figure. Negatively charged areas are shown singly cross-hatched; it is evident that the large tripartite negative region on the left subunit, derived from Glu95 (middle), Glu97 (top), and Glu109 (bottom), will close up against the more compact negative region on the right subunit, derived from Glu106.
Biophysical Journal  , DOI: ( /S (98) )
Copyright © 1998 The Biophysical Society Terms and Conditions