User:David McDonald/Replication Termination Protein: Difference between revisions

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== Structure ==
== Structure ==
<Structure load='1BM9' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<Structure load='1BM9' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<scene name='User:David_McDonald/Replication_Termination_Protein/Rainbow_monomer/3'>RTP</scene> contains 122 amino acid residues and is an example of a winged helix structure, in the α+β protein folding family, containing <scene name='User:David_McDonald/Replication_Termination_Protein/Alpha_helices/2'>four α-helices</scene> and <scene name='User:David_McDonald/Replication_Termination_Protein/Beta_sheets/1'>three β-strands</scene> (1).
<scene name='User:David_McDonald/Replication_Termination_Protein/Rainbow_monomer/6'>RTP</scene> contains 122 amino acid residues and is an example of a winged helix structure, in the α+β protein folding family, containing <scene name='User:David_McDonald/Replication_Termination_Protein/Alpha_helices/5'>four α-helices</scene> and <scene name='User:David_McDonald/Replication_Termination_Protein/Beta_sheets/1'>three β-strands</scene> (1).
In a cell, RTP exists as a homodimer, where the monomer subunits are tightly associated through antiparallel coiled-coil interactions between the<scene name='User:David_McDonald/Replication_Termination_Protein/Dimerisation_domain/2'>C-terminal α-helices</scene>.
In a cell, RTP exists as a homodimer, where the monomer subunits are tightly associated through antiparallel coiled-coil interactions between the<scene name='User:David_McDonald/Replication_Termination_Protein/Dimerisation_domain/2'>C-terminal α-helices</scene>.


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