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User:Eric Martz/5eon
From Proteopedia
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<StructureSection size='[300,400]' side='right' caption='Biological unit of [[5eon]].' scene='73/733958/Hexamer_of_5eon/1'> | <StructureSection size='[300,400]' side='right' caption='Biological unit of [[5eon]].' scene='73/733958/Hexamer_of_5eon/1'> | ||
| - | The [[biological unit]] of [[5eon]] is a crystallographic structure of 6 alpha helices assembled into a fiber with a hydrophobic core<ref name="5eon">PMID: 27192036</ref>. The individual peptides are synthetic and were designed to assemble in this manner, with a hydrophotic core rich in phenylalanine. The crystal structure has a [[resolution]] of 1.7 Å (very good), and an [[Rfree]] of 0.22, which is average for this resolution, indicating that the model is reliable. | + | The [[biological unit]] of [[5eon]] (<scene name='73/733958/Hexamer_of_5eon/1'>restore initial scene</scene>) is a crystallographic structure of 6 alpha helices assembled into a fiber with a hydrophobic core<ref name="5eon">PMID: 27192036</ref>. The individual peptides are synthetic and were designed to assemble in this manner, with a hydrophotic core rich in phenylalanine. The crystal structure has a [[resolution]] of 1.7 Å (very good), and an [[Rfree]] of 0.22, which is average for this resolution, indicating that the model is reliable. |
The <scene name='73/733958/Hexamer_of_5eon/3'>aromatic rings of Phe pack in the core</scene>. The Phe rings (<font color="#686868">'''dark gray'''</font>) are surrounded by <scene name='73/733958/Hexamer_of_5eon/4'>hydrophobic sidechains of Ile</scene> (<font color="#909090">'''light gray'''</font>). | The <scene name='73/733958/Hexamer_of_5eon/3'>aromatic rings of Phe pack in the core</scene>. The Phe rings (<font color="#686868">'''dark gray'''</font>) are surrounded by <scene name='73/733958/Hexamer_of_5eon/4'>hydrophobic sidechains of Ile</scene> (<font color="#909090">'''light gray'''</font>). | ||
Revision as of 19:26, 4 June 2016
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References and Notes
- ↑ Spencer RK, Hochbaum AI. X-ray Crystallographic Structure and Solution Behavior of an Antiparallel Coiled-Coil Hexamer Formed by de Novo Peptides. Biochemistry. 2016 May 27. PMID:27192036 doi:http://dx.doi.org/10.1021/acs.biochem.6b00201
