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is located at 75-432 nt on the viral RNA. Elongation of the coat proteins
occurs in 5
′→
′
′→
′
′
direction is
considerably slower (Butler & Klug, 1972; Culver, 2002; Fraenkel-Conrat &
Williams, 1955; Klug, 1972, 1999).
3
and 3
5
direction; assembly toward the 3
Figure 3.7
(TMV) proteins used in
reconstitution experiments. Top panel shows disk-shaped particles with central
holes. Bottom panel shows rod-shaped particles with morphology identical to that
of normal TMV. Reproduced from Fraenkel-Conrat , H., and Williams , R. C. (1955)
Reconstitution of active tobacco mosaic virus from its inactive protein and nucleic
acid components,
Electron micrographs of
Tobacco mosaic virus
Proc. Natl. Acad. Sci. USA
,
41
(10), 690-698.
Coat protein monomers can also be self-assembled into rods without
nucleic acid. These methods have been exploited to fabricate self-
assembled light harvesting systems. Different fluorescent dye-labeled coat
proteins were self-assembled into either disks or rods. During this process,
the different fluorescent dyes (i.e., chromophores) are brought into near
proximity, allowing energy transfer between the chromophores (Miller
et
al.
, 2007). This system may be further developed for the construction of a
photovoltaic device and is discussed in Chapter 4.
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