Examples of capsid

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In conclusion, internal genome pressure is one of the key determining factors for phage infectivity and capsid stability.
However, viroids are not enclosed in protein capsids.
The monomer consists of a central eight-stranded antiparallel barrel that is topologically similar to other viral capsid proteins.
However, structural studies on virus capsids and coat proteins propose that there are only a limited number of ways to construct a viral protein coat.
A viral particle shell or capsid is composed of many building blocks, each of which may consist of several identical or different protein monomers.
Formation of the icosahedral capsid is thought to occur on these membranes.
Within this approach, the capsid is described by two elastic constants characterizing the in plane stretching of the shell, and its bending out of plane.
In the latter case, the capsid is covered with a lipid envelope that fuses with the host cell plasma membrane.
The deformation of the capsid is linear until a critical deformation is reached, after which a sudden decrease in capsid height can be observed.
The maximum capsid breaking force was also determined.
However, this method does not allow precise quantification of capsid robustness.
This type of model allows prediction of the critical breaking force of empty and full capsids.
The outer capsid has an ordered structure with icosahedral symmetry.
At the same time, maximum indentation is similar for all four viruses above, about 20-30 % of capsid height.
A thermally induced phase transition in a viral capsid transforms the hexamers, leaving the pentamers unchanged.
The most notable is in the structure and function of the two outer capsid proteins.
The virion contains a nucleocapsid core of 20 -30 nm composed of a single capsid protein.
Extensive hydrogen-bond networks between the capsid and the saccharide ligands have been predicted based on the electron density map.

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