Sandbox Reserved 428: Difference between revisions
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===Overall Structure=== | ===Overall Structure=== | ||
EcoRV endonuclease is a dimer made up of two monomers. Each monomer depicted <scene name='Sandbox_Reserved_428/Dimer_complex/2'>here</scene> is shown in green and purple. | |||
<scene name='Sandbox_Reserved_428/Alpha_helixes_and_beta_sheets/1'>Alpha Helixes and Beta Sheets</scene> | <scene name='Sandbox_Reserved_428/Alpha_helixes_and_beta_sheets/1'>Alpha Helixes and Beta Sheets</scene> | ||
===Binding Interactions=== | ===Binding Interactions=== | ||
Revision as of 21:36, 3 April 2012
| This Sandbox is Reserved from January 19, 2016, through August 31, 2016 for use for Proteopedia Team Projects by the class Chemistry 423 Biochemistry for Chemists taught by Lynmarie K Thompson at University of Massachusetts Amherst, USA. This reservation includes Sandbox Reserved 425 through Sandbox Reserved 439. |
YourMacromolecule
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Introduction
Outline -found in e. coli -is a type II restriction endonuclease/enzyme -explain restriction enzymes---cut DNA -explain differences between type II and others -works in presence of Mg(2+) -cuts specific section of DNA
Overall Structure
EcoRV endonuclease is a dimer made up of two monomers. Each monomer depicted here is shown in green and purple.
Binding Interactions
The interactions that hold this protein together are aided by the interaction of Mg2+ atoms. They hold together the active site of the dimers. This is a charge-charge interaction, since the Magnesium has a 2+ charge. The oxygen atoms also have a partial negative charge which interactions with this positive charge.
Additional Features
Credits
Introduction - Jesse
Overall Structure - Nicole
Drug Binding Site - Julia
Additional Features - Sam
