Sandbox Reserved 434
From Proteopedia
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[[Student Projects for UMass Chemistry 423 Spring 2016]] | [[Student Projects for UMass Chemistry 423 Spring 2016]] | ||
| + | <StructureSection load='4CYG' size='350' side='right' caption='caption for Molecular Playground (PDB entry [[4CYG]])' scene=''> | ||
==Introduction== | ==Introduction== | ||
| - | <Structure load='4cyg' size='300' frame='true' align='right' caption='4cyg, Insert caption here' scene='Insert optional scene name here' /> | ||
The two protein subunits possess dense regions of <scene name='48/483891/Secondary_structure/1'>beta strands and alpha helices.</scene> | The two protein subunits possess dense regions of <scene name='48/483891/Secondary_structure/1'>beta strands and alpha helices.</scene> | ||
Main points: | Main points: | ||
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- A small paragraph on its discovery | - A small paragraph on its discovery | ||
- The broad impact of the protein (what happens if it loses function?) | - The broad impact of the protein (what happens if it loses function?) | ||
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==Overall Structure== | ==Overall Structure== | ||
| - | <Structure load='4cyg' size='300' frame='true' align='right' caption='4cyg, insert caption here' scene='Insert optional scene name here' /> | ||
- 506 total residues, 87 missing | - 506 total residues, 87 missing | ||
- Two chains, each with many alpha helices and beta sheets | - Two chains, each with many alpha helices and beta sheets | ||
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==Binding Interactions== | ==Binding Interactions== | ||
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| - | <Structure load='4cyg' size='300' frame='true' align='right' caption='4cyg, Insert caption here' scene='Insert optional scene name here' /> | ||
<scene name='48/483891/Alpha_and_beta_structures/2'>Alpha and Beta Structures</scene> | <scene name='48/483891/Alpha_and_beta_structures/2'>Alpha and Beta Structures</scene> | ||
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==Additional Features== | ==Additional Features== | ||
| - | <Structure load='1a84' size='300' frame='true' align='right' caption='pdbcode, Insert caption here' scene='polarity' /> | ||
<scene name='48/483891/Polarity/1'>The purple chains represent the polar and therefore hydrophilic regions of 4CYG and the grey chains represent the nonpolar hydrophobic regions of 4CYG.</scene> | <scene name='48/483891/Polarity/1'>The purple chains represent the polar and therefore hydrophilic regions of 4CYG and the grey chains represent the nonpolar hydrophobic regions of 4CYG.</scene> | ||
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==Quiz Question 1== | ==Quiz Question 1== | ||
| - | <Structure load='1a84' size='300' frame='true' align='right' caption='pdbcode, Insert caption here' scene='Insert optional scene name here' /> | ||
- Additional research needed to formulate question (may potentially pertain to structure-substrate interaction) | - Additional research needed to formulate question (may potentially pertain to structure-substrate interaction) | ||
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==See Also== | ==See Also== | ||
Revision as of 22:23, 2 March 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. |
Pantetheinase (4CYG)[1]
by [Luke Schnitzler, Patrick Tonne, Owen O'Connor, Tyler Russell, Nicholas Sant]
Student Projects for UMass Chemistry 423 Spring 2016
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