Sandbox Reserved 426
From Proteopedia
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Revision as of 15:24, 24 February 2016
| 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. |
Contents |
Structure of Oligonucleotide/Drug complex (1xcs)
by Michael Beauregard, Annie Burton, Jianlong Li, Daniel Marco, and Nathaneal Park
Student Projects for UMass Chemistry 423 Spring 2016
Introduction
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Notice the similarity in shape and side chains.
Overall Structure
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The 1xcs (model at right) protein is a small, simple globular protein lacking any clear secondary beta sheets or alpha helices. The protein consists of two non-identical dimers. A simplified model of 1xcs is shown with the side chains removed for clarity. The protein can be followed from N to C terminus following along each strand from blue to red. Note that the strands are antiparallel where they are non-covalently bound. visualizes this bonding in the middle region of the protein, again following each strand from blue to red from N to C terminus.
Binding Interactions
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Additional Features
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Quiz Question 1
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A unique site is the __ ion found associated with the , which gives additional strength to the guanine–Co2+–guanine interaction. A Mg2+ B Co2+ C Ba2+ D Mg2+
See Also
Credits
Introduction - Daniel Marco
Overall Structure - Nathaneal Park
Drug Binding Site - name of team member
Additional Features - name of team member
Quiz Question 1 - Jianlong Li
