Sandbox 206: Difference between revisions

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==== Primary and Secondary structure ====

Venus is a 27 kDa protein (26 875,50Da) consisting of 239 residues and form a secondary structure of 7 <scene name='Sandbox_206/Alpha_helix/1'>α-helix</scene> (2 in the center of the molecule) and <scene name='Sandbox_206/Sheet/2'> one eleven-stranded β-pleated sheet</scene>. This molecule is monomeric. Venus has many common point with the GFP and also with the EYFP. In all three structures compared, the cross-section taken perpendicularly to the long axis of the barrel is not perfectly circular but rather <scene name='Sandbox_206/Oval/1'>oval</scene> in shape. While the longer diameter of the oval cross-section of all three proteins is identical (23.8 Å measured from distances of four Cα pairs), the shorter diameter differs between EYFP (22.3 Å) and Venus (21.9 Å). The difference in the oval shape between these yellow variants is closely related to the packing of inte- rior amino acid residues and influences the integrity of dimer interface.

Venus is a 27 kDa protein (26 875,50Da) consisting of 239 residues and form a secondary structure of 7 <scene name='Sandbox_206/Alpha_helix/1'>α-helix</scene> (2 in the center of the molecule) and <scene name='Sandbox_206/Sheet/2'>one eleven-stranded β-pleated sheet</scene>. This molecule is monomeric. Venus has many common point with the GFP and also with the EYFP. In all three structures compared, the cross-section taken perpendicularly to the long axis of the barrel is not perfectly circular but rather <scene name='Sandbox_206/Oval/1'>oval</scene> in shape. While the longer diameter of the oval cross-section of all three proteins is identical (23.8 Å measured from distances of four Cα pairs), the shorter diameter differs between EYFP (22.3 Å) and Venus (21.9 Å). The difference in the oval shape between these yellow variants is closely related to the packing of inte- rior amino acid residues and influences the integrity of dimer interface.

==== The Chromophore ====

Sandbox 206: Difference between revisions

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 ==== Primary and Secondary structure ====
-Venus is a 27 kDa protein (26 875,50Da) consisting of 239 residues and form a secondary structure of 7 <scene name='Sandbox_206/Alpha_helix/1'>α-helix</scene> (2 in the center of the molecule) and <scene name='Sandbox_206/Sheet/2'> one eleven-stranded β-pleated sheet</scene>. This molecule is monomeric. Venus has many common point with the GFP and also with the EYFP. In all three structures compared, the cross-section taken perpendicularly to the long axis of the barrel is not perfectly circular but rather <scene name='Sandbox_206/Oval/1'>oval</scene> in shape. While the longer diameter of the oval cross-section of all three proteins is identical (23.8 Å measured from distances of four Cα pairs), the shorter diameter differs between EYFP (22.3 Å) and Venus (21.9 Å). The difference in the oval shape between these yellow variants is closely related to the packing of inte- rior amino acid residues and influences the integrity of dimer interface.
+Venus is a 27 kDa protein (26 875,50Da) consisting of 239 residues and form a secondary structure of 7 <scene name='Sandbox_206/Alpha_helix/1'>α-helix</scene> (2 in the center of the molecule) and <scene name='Sandbox_206/Sheet/2'>one eleven-stranded β-pleated sheet</scene>. This molecule is monomeric. Venus has many common point with the GFP and also with the EYFP. In all three structures compared, the cross-section taken perpendicularly to the long axis of the barrel is not perfectly circular but rather <scene name='Sandbox_206/Oval/1'>oval</scene> in shape. While the longer diameter of the oval cross-section of all three proteins is identical (23.8 Å measured from distances of four Cα pairs), the shorter diameter differs between EYFP (22.3 Å) and Venus (21.9 Å). The difference in the oval shape between these yellow variants is closely related to the packing of inte- rior amino acid residues and influences the integrity of dimer interface.
 ==== The Chromophore ====