Sandbox Reserved 1561: Difference between revisions
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<scene name='82/823085/Tertiary_structure_view/1'>Tertiary Structure View</scene> Bap1 from V. cholerae is composed of a beta-prism that attaches to blade six of the eight-bladed beta-propeller. The beta-prism is an accessory domain to the eight-bladded beta-propeller domain, these two domains make up the tertiary structure of the protein. | <scene name='82/823085/Tertiary_structure_view/1'>Tertiary Structure View</scene> Bap1 from V. cholerae is composed of a beta-prism that attaches to blade six of the eight-bladed beta-propeller. The beta-prism is an accessory domain to the eight-bladded beta-propeller domain, these two domains make up the tertiary structure of the protein. | ||
<scene name='82/823085/Major_secondary_structure_view/1'>Major Secondary Structures </scene> of Bap1 can been viewed in the beta-propeller and throughout the protein as beta-sheets. Shown in red are the four anti-parallel beta-sheets that construct each blade of the eight-bladed beta-propeller of Bap1. | <scene name='82/823085/Major_secondary_structure_view/1'>Major Secondary Structures </scene> of Bap1 can been viewed in the beta-propeller and throughout the protein as beta-sheets. Shown in red are the four anti-parallel beta-sheets that construct each blade of the eight-bladed beta-propeller of Bap1. <scene name='82/823085/Full_secondary_structure_view/1'>Full Secondary Structure View of Bap1</scene> | ||
<scene name='82/823085/Bap1_hydrophobic_polar_view/1'>Bap1 Hydrophobic Polar View</scene> Bap1 is an insoluble protein at full length and requires a deletion of a hydrophobic 57-amino acid chain along with an inset to take its place, which forms the beta-prism domain within blade-six of the eight-bladed beta-propeller. The beta-prism domain contributes the Bap1 solubility and expression eventually yielding the proteins crystal structure, with is a major construct of protein. <ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref> | <scene name='82/823085/Bap1_hydrophobic_polar_view/1'>Bap1 Hydrophobic Polar View</scene> Bap1 is an insoluble protein at full length and requires a deletion of a hydrophobic 57-amino acid chain along with an inset to take its place, which forms the beta-prism domain within blade-six of the eight-bladed beta-propeller. The beta-prism domain contributes the Bap1 solubility and expression eventually yielding the proteins crystal structure, with is a major construct of protein. <ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref> | ||
