Sandbox Reserved 1798: Difference between revisions

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You can see the two-part portion of the protein. The protein has been made somewhat<scene name='95/954095/Color_change/5'> transparent</scene> so you can see the substrate within the ligand.

Two linkers connect two similar lobes. Alpha helices surround a beta-sheet. The C-terminal lobe inserts after β-strand number four on the N-terminal lobe, as many VFT proteins do. A long, 90-amino-acid-long α-clamp wraps around lobe 1’s back side. A number of hydrophobic amino acid contacts on helix α9, the loop connecting α11 and α12, and the C-terminus. There is a π-bulge on center α6 helix of the second lobe that has hydrophobic interactions between the α-clamp and α6.

Two linkers connect two similar lobes. Alpha helices surround a beta-sheet. The C-terminal lobe inserts after β-strand number four on the N-terminal lobe, as many VFT proteins do. A long, 90-amino-acid-long α-clamp wraps around lobe 1’s back side. A number of <scene name='95/954095/Hydrophobic_region/1'>hydrophobic amino acid contacts</scene> on helix α9, the loop connecting α11 and α12, and the C-terminus. There is a π-bulge on center α6 helix of the second lobe that has hydrophobic interactions between the α-clamp and α6. (Hydrophobic areas are shown in green, the rest of the molecule is in brown.)

Sandbox Reserved 1798: Difference between revisions

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Revision as of 00:23, 28 April 2023 view source Julia Galasso (talk \| contribs) 35 edits No edit summary ← Older edit		Revision as of 00:31, 28 April 2023 view source Julia Galasso (talk \| contribs) 35 edits No edit summary Newer edit →
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	You can see the two-part portion of the protein. The protein has been made somewhat<scene name='95/954095/Color_change/5'> transparent</scene> so you can see the substrate within the ligand.		You can see the two-part portion of the protein. The protein has been made somewhat<scene name='95/954095/Color_change/5'> transparent</scene> so you can see the substrate within the ligand.

	Two linkers connect two similar lobes. Alpha helices surround a beta-sheet. The C-terminal lobe inserts after β-strand number four on the N-terminal lobe, as many VFT proteins do. A long, 90-amino-acid-long α-clamp wraps around lobe 1’s back side. A number of hydrophobic amino acid contacts on helix α9, the loop connecting α11 and α12, and the C-terminus. There is a π-bulge on center α6 helix of the second lobe that has hydrophobic interactions between the α-clamp and α6.		Two linkers connect two similar lobes. Alpha helices surround a beta-sheet. The C-terminal lobe inserts after β-strand number four on the N-terminal lobe, as many VFT proteins do. A long, 90-amino-acid-long α-clamp wraps around lobe 1’s back side. A number of <scene name='95/954095/Hydrophobic_region/1'>hydrophobic amino acid contacts</scene> on helix α9, the loop connecting α11 and α12, and the C-terminus. There is a π-bulge on center α6 helix of the second lobe that has hydrophobic interactions between the α-clamp and α6. (Hydrophobic areas are shown in green, the rest of the molecule is in brown.)