User:Eric Martz/5eon: Difference between revisions
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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 22:26, 4 June 2016
The biological unit of 5eon () is a crystallographic structure of 6 alpha helices assembled into a fiber with a hydrophobic core[1]. 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 . The Phe rings (dark gray) are surrounded by (light gray). The charges form on the surface, reminiscent of Xiao's theoretical model of the Geobacter sulfurreducens pilus. SequenceThe peptide sequence is constructed from 4 copies of heptad E L/F K A I A Q/K/W The amino-terminal Glu is acetylated, removing its positive charge. The C-terminal Lys is amidated, removing its negative charge. Here is the sequence of one complete peptide (29 amino acids) showing the heptad repeats. ELKAIAQ EFKAIAK EFKAIAW EFKAIAQ K
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References and NotesReferences 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