User:Eric Martz/5eon
From Proteopedia
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The <scene name='73/733958/Hexamer_of_5eon/5'>surface of the fiber</scene> is mostly charged <font color="blue">'''Lys+'''</font> and <font color="red">'''Glu-'''</font> sidechains, with an occasional Trp or Gln, interspersed with Ala (spheres). | The <scene name='73/733958/Hexamer_of_5eon/5'>surface of the fiber</scene> is mostly charged <font color="blue">'''Lys+'''</font> and <font color="red">'''Glu-'''</font> sidechains, with an occasional Trp or Gln, interspersed with Ala (spheres). | ||
- | The charges form <scene name='73/733958/Hexamer_of_5eon/2'>helices of opposite charge</scene> on the surface, reminiscent of [[User:Ke Xiao/Geobacter pilus models|Xiao's theoretical model of the ''Geobacter sulfurreducens'' pilus]]. Unlike Xiao's model, none of these form salt bridges (a few opposite charges are water-bridged). [[Cation-pi interactions]] involving Phe cannot form since Phe is buried and Lys is on the surface. A few cation-pi interactions may form between Trp on the surface and Lys. | + | The charges form <scene name='73/733958/Hexamer_of_5eon/2'>helices of opposite charge</scene> on the surface, reminiscent of [[User:Ke Xiao/Geobacter pilus models|Xiao's theoretical model of the ''Geobacter sulfurreducens'' pilus]]. Terminal charges on the chains were blocked (see below). Unlike Xiao's model, none of these form salt bridges (a few opposite charges are water-bridged). |
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+ | [[Cation-pi interactions]] involving Phe cannot form since Phe is buried and Lys is on the surface. A few cation-pi interactions may form between Trp on the surface and Lys. | ||
==Sequence== | ==Sequence== |
Revision as of 16:09, 17 June 2016
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View in FirstGlance
- Asymmetric unit (trimer) of 5eon in FirstGlance
- The biological unit is available from within FirstGlance (Resources tab), but for convenience: Biological unit (hexamer) of 5eon in FirstGlance
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