Sandbox 47
From Proteopedia
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BPTI is a single chain polypeptide with 58 amino acids. It's secondary structure includes one <scene name='Sandbox_47/Sheet_ribbon/1'>beta sheet</scene> and <scene name='Sandbox_47/Helices/1'>two alpha helices</scene>. The beta sheet consists of <scene name='Sandbox_47/Sheet_side_chains/1'>two antiparallel strands</scene> (Ile18 to Asn 24 and Leu 29 to Tyr 35) with a <scene name='Sandbox_47/Turn/1'>beta hairpin</scene> consisting of four residues (Ala 25, Lys 26, Ala 27, Gly 28). Alpha helix | BPTI is a single chain polypeptide with 58 amino acids. It's secondary structure includes one <scene name='Sandbox_47/Sheet_ribbon/1'>beta sheet</scene> and <scene name='Sandbox_47/Helices/1'>two alpha helices</scene>. The beta sheet consists of <scene name='Sandbox_47/Sheet_side_chains/1'>two antiparallel strands</scene> (Ile18 to Asn 24 and Leu 29 to Tyr 35) with a <scene name='Sandbox_47/Turn/1'>beta hairpin</scene> consisting of four residues (Ala 25, Lys 26, Ala 27, Gly 28). Alpha helix | ||
<scene name='Sandbox_47/H1/1'>H1</scene> is 4 residues (Asp 3 to Cys 6), and <scene name='Sandbox_47/H2/1'>H2</scene> is 8 residues (Ala 48 to Cys 55). There are three intrachain disulfide bonds in this polypeptide, one between <scene name='Sandbox_47/Ds1/1'>Cys 5 and Cys 55</scene>, one between <scene name='Sandbox_47/Ds2/1'>Cys 14 and Cys 38</scene>, and one between <scene name='Sandbox_47/Ds3/1'>Cys 30 and Cys 51</scene>. This protein has a <scene name='Sandbox_47/Hydrophobic_core/1'>hydrophobic core</scene> (gray) with polar and charged residues (purple) extending mostly on the <scene name='Sandbox_47/Hydrophobic_dist/3'>surface</scene>. | <scene name='Sandbox_47/H1/1'>H1</scene> is 4 residues (Asp 3 to Cys 6), and <scene name='Sandbox_47/H2/1'>H2</scene> is 8 residues (Ala 48 to Cys 55). There are three intrachain disulfide bonds in this polypeptide, one between <scene name='Sandbox_47/Ds1/1'>Cys 5 and Cys 55</scene>, one between <scene name='Sandbox_47/Ds2/1'>Cys 14 and Cys 38</scene>, and one between <scene name='Sandbox_47/Ds3/1'>Cys 30 and Cys 51</scene>. This protein has a <scene name='Sandbox_47/Hydrophobic_core/1'>hydrophobic core</scene> (gray) with polar and charged residues (purple) extending mostly on the <scene name='Sandbox_47/Hydrophobic_dist/3'>surface</scene>. | ||
| - | BPTI interacts with 98 <scene name='Sandbox_47/Water/1'>water molecules</scene> as well as 4 <scene name='Sandbox_47/Ligands/1'>sulfate anion ligands</scene>. Ligand <scene name='Sandbox_47/Ligand_61/1'>61 | + | BPTI interacts with 98 <scene name='Sandbox_47/Water/1'>water molecules</scene> as well as 4 <scene name='Sandbox_47/Ligands/1'>sulfate anion ligands</scene>. Ligand <scene name='Sandbox_47/Ligand_61/1'>61</scene> binds the protein through hydrophobic interactions between Glu 7, Lys 7, and Phe 41, as well as through 3 hydrogen bonds to Arg 42. Three water molecules are also interact with this ligand. Ligand <scene name='Sandbox_47/Ligand_62/1'>62 </scene> has hydrophobic interaction with Ala 40, two hydrogen bonds with Arg 20, and one hydrogen bond with Tyr 35. |
Revision as of 19:29, 29 October 2010
| Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013. |
Bovine Pancreatic Trypsin Inhibitor (BPTI) Mutant with Altered Binding Loop Sequence
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BPTI is a single chain polypeptide with 58 amino acids. It's secondary structure includes one and . The beta sheet consists of (Ile18 to Asn 24 and Leu 29 to Tyr 35) with a consisting of four residues (Ala 25, Lys 26, Ala 27, Gly 28). Alpha helix is 4 residues (Asp 3 to Cys 6), and is 8 residues (Ala 48 to Cys 55). There are three intrachain disulfide bonds in this polypeptide, one between , one between , and one between . This protein has a (gray) with polar and charged residues (purple) extending mostly on the . BPTI interacts with 98 as well as 4 . Ligand binds the protein through hydrophobic interactions between Glu 7, Lys 7, and Phe 41, as well as through 3 hydrogen bonds to Arg 42. Three water molecules are also interact with this ligand. Ligand has hydrophobic interaction with Ala 40, two hydrogen bonds with Arg 20, and one hydrogen bond with Tyr 35.
