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/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, which forms the beta-prism domain within blade-six of the eight-bladed beta-propeller. | <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, which forms the beta-prism domain within blade-six of the eight-bladed beta-propeller. <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='82/823085/57aa_insertion/1'>57aa Insertion</scene> is located in the beta-prism of Bap1 between residues 414-473. Bap1 eight-bladed beta-propeller is insoluble until the beta-prism is attached in the loop of blade six of the beta-propeller. Once the insertion and beta-prism are bound to the beta-propeller Bap1 improves in soluble expression. <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='82/823085/57aa_insertion/1'>57aa Insertion</scene> is located in the beta-prism of Bap1 between residues 414-473. Bap1 eight-bladed beta-propeller is insoluble until the beta-prism is attached in the loop of blade six of the beta-propeller. Once the insertion and beta-prism are bound to the beta-propeller Bap1 improves in soluble expression. <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> | ||
