Sandbox Reserved 489: Difference between revisions

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The precursor of renin is a 406 amino acid residue protein. <scene name='Sandbox_Reserved_489/Signal_domain/1'>Residues 1-23</scene> are a signal peptide sequence and residues 24-66 are cleaved to produce the mature 340 amino acid residue <scene name='Sandbox_Reserved_489/Mature_renin/1'>mature renin</scene>. The secondary structural elements of renin include <scene name='Sandbox_Reserved_489/Betasheetscolors/1'>29 antiparallel beta sheets</scene>, <scene name='Sandbox_Reserved_489/Betabridges/1'>3 beta bridges</scene>, <scene name='Sandbox_Reserved_489/Alphahelixes/1'>4 alpha helices</scene>, <scene name='Sandbox_Reserved_489/310heleices/1'>2 3-10 helices</scene>, and <scene name='Sandbox_Reserved_489/Turns/1'>18 turns</scene>. The most impressive structural feature of renin is the <scene name='Sandbox_Reserved_489/Betasheetspiral/1'>antiparallel beta sheet elongated spiral barrel</scene>. <scene name='Sandbox_Reserved_489/Hydrophobichydrophillic/1'>Hydrophilic and hydrophobic residues</scene> are practically evenly distributed throughout renin. The alternating hydrophilic and hydrophobic residues most likely assist in folding of the unique spiral structure.

The precursor of renin is a 406 amino acid residue protein. <scene name='Sandbox_Reserved_489/Signal_domain/1'>Residues 1-23</scene> are a signal peptide sequence and residues 24-66 are cleaved to produce the mature 340 amino acid residue <scene name='Sandbox_Reserved_489/Mature_renin/1'>mature renin</scene>. The secondary structural elements of renin include <scene name='Sandbox_Reserved_489/Betasheetscolors/1'>29 antiparallel beta sheets</scene>, <scene name='Sandbox_Reserved_489/Betabridges/1'>3 beta bridges</scene>, <scene name='Sandbox_Reserved_489/Alphahelixes/1'>4 alpha helices</scene>, <scene name='Sandbox_Reserved_489/310heleices/1'>2 3-10 helices</scene>, and <scene name='Sandbox_Reserved_489/Turns/1'>18 turns</scene>. The most impressive structural feature of renin is the <scene name='Sandbox_Reserved_489/Betasheetspiral/1'>antiparallel beta sheet elongated spiral barrel</scene>. <scene name='Sandbox_Reserved_489/Hydrophobichydrophillic/1'>Hydrophilic and hydrophobic residues</scene> are practically evenly distributed throughout renin. The alternating hydrophilic and hydrophobic residues most likely assist in folding of the unique spiral structure. The active site of renin contains two essential <scene name='Sandbox_Reserved_489/Activesiteasps2/2'>aspartate residues</scene>.

Sandbox Reserved 489: Difference between revisions

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Revision as of 20:12, 14 April 2012 view source Matthew Tugwell (talk \| contribs) 119 edits No edit summary ← Older edit		Revision as of 20:43, 14 April 2012 view source Matthew Tugwell (talk \| contribs) 119 edits No edit summary Newer edit →
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	<Structure load='2ren' size='400' frame='true' align='right' caption='Mature Renin' scene='Insert optional scene name here' />		<Structure load='2ren' size='400' frame='true' align='right' caption='Mature Renin' scene='Insert optional scene name here' />
	The precursor of renin is a 406 amino acid residue protein. <scene name='Sandbox_Reserved_489/Signal_domain/1'>Residues 1-23</scene> are a signal peptide sequence and residues 24-66 are cleaved to produce the mature 340 amino acid residue <scene name='Sandbox_Reserved_489/Mature_renin/1'>mature renin</scene>. The secondary structural elements of renin include <scene name='Sandbox_Reserved_489/Betasheetscolors/1'>29 antiparallel beta sheets</scene>, <scene name='Sandbox_Reserved_489/Betabridges/1'>3 beta bridges</scene>, <scene name='Sandbox_Reserved_489/Alphahelixes/1'>4 alpha helices</scene>, <scene name='Sandbox_Reserved_489/310heleices/1'>2 3-10 helices</scene>, and <scene name='Sandbox_Reserved_489/Turns/1'>18 turns</scene>. The most impressive structural feature of renin is the <scene name='Sandbox_Reserved_489/Betasheetspiral/1'>antiparallel beta sheet elongated spiral barrel</scene>. <scene name='Sandbox_Reserved_489/Hydrophobichydrophillic/1'>Hydrophilic and hydrophobic residues</scene> are practically evenly distributed throughout renin. The alternating hydrophilic and hydrophobic residues most likely assist in folding of the unique spiral structure.		The precursor of renin is a 406 amino acid residue protein. <scene name='Sandbox_Reserved_489/Signal_domain/1'>Residues 1-23</scene> are a signal peptide sequence and residues 24-66 are cleaved to produce the mature 340 amino acid residue <scene name='Sandbox_Reserved_489/Mature_renin/1'>mature renin</scene>. The secondary structural elements of renin include <scene name='Sandbox_Reserved_489/Betasheetscolors/1'>29 antiparallel beta sheets</scene>, <scene name='Sandbox_Reserved_489/Betabridges/1'>3 beta bridges</scene>, <scene name='Sandbox_Reserved_489/Alphahelixes/1'>4 alpha helices</scene>, <scene name='Sandbox_Reserved_489/310heleices/1'>2 3-10 helices</scene>, and <scene name='Sandbox_Reserved_489/Turns/1'>18 turns</scene>. The most impressive structural feature of renin is the <scene name='Sandbox_Reserved_489/Betasheetspiral/1'>antiparallel beta sheet elongated spiral barrel</scene>. <scene name='Sandbox_Reserved_489/Hydrophobichydrophillic/1'>Hydrophilic and hydrophobic residues</scene> are practically evenly distributed throughout renin. The alternating hydrophilic and hydrophobic residues most likely assist in folding of the unique spiral structure. The active site of renin contains two essential <scene name='Sandbox_Reserved_489/Activesiteasps2/2'>aspartate residues</scene>.