User:David Jung/BCHM3981 RTP Tus

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RTP Tus test
RTP Tus test
== History ==
== History ==
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'''Differential binding affinity model'''
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For each terminator site (''Ter'' site), two dimers of RTP bind. Each dimer binds to each half site present in a terminator site. It was hypothesised that the RTP dimer binding to the half site located in the "blocking" site binds tightly while the dimer binding to the "permissive" site binds less tightly to the site. However, after a series of experiments using mutant forms of terminator sites that contain RTP binding half sites with differential binding affinity, it was concluded that this differential binding affinity model cannot solely explain the polarity of termination.
== Structure ==
== Structure ==
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<Structure load='2I05' size='500' frame='true' align='right' caption='Tus' scene='Insert optional scene name here' />
 
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The structure of Tus protein was first determined by
 
<Structure load='2EFW' size='500' frame='true' align='right' caption='RTP' scene='Insert optional scene name here' />
<Structure load='2EFW' size='500' frame='true' align='right' caption='RTP' scene='Insert optional scene name here' />
== Function ==
== Function ==

Revision as of 00:43, 13 May 2011

RTP Tus test

History

Differential binding affinity model For each terminator site (Ter site), two dimers of RTP bind. Each dimer binds to each half site present in a terminator site. It was hypothesised that the RTP dimer binding to the half site located in the "blocking" site binds tightly while the dimer binding to the "permissive" site binds less tightly to the site. However, after a series of experiments using mutant forms of terminator sites that contain RTP binding half sites with differential binding affinity, it was concluded that this differential binding affinity model cannot solely explain the polarity of termination.

Structure

RTP

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Function

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David Jung

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