Sandbox Reserved 195: Difference between revisions
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Hydrogen bonding and hydrophobic interactions play a major role in the structure of RNase S. <ref name="Kim" /> There are 84 water molecules present, with 8 of these specifically connecting S peptide and S protein. Some of these water molecules are also conserved throughout all RNase derivatives. Hydrophobic interactions between residues Phe 8, Met 13, His 12, Ala 4 are essential in holding the S Peptide in place. In addition to these residues, Asp 14 is also important in peptide-protein binding, as represented in the 2D picture. In the picture, it appears that the protein and peptide are not connected; this is because the bond cleavage between residues 20 and 21 of RNase A has already occurred. Additionally RNase S has a rigid hydrophobic core; one-third of the surface of the core is made up of the S peptide. The surrounding loops have more flexibility. | Hydrogen bonding and hydrophobic interactions play a major role in the structure of RNase S. <ref name="Kim" /> There are 84 water molecules present, with 8 of these specifically connecting S peptide and S protein. Some of these water molecules are also conserved throughout all RNase derivatives. Hydrophobic interactions between residues Phe 8, Met 13, His 12, Ala 4 are essential in holding the S Peptide in place. In addition to these residues, Asp 14 is also important in peptide-protein binding, as represented in the 2D picture. In the picture, it appears that the protein and peptide are not connected; this is because the bond cleavage between residues 20 and 21 of RNase A has already occurred. Additionally RNase S has a rigid hydrophobic core; one-third of the surface of the core is made up of the S peptide. The surrounding loops have more flexibility. | ||
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[[Image:surface view of rnase s.png]] | [[Image:surface view of rnase s.png]] | ||
{{Quote box | {{Quote box | ||
| quote = | | quote = The image above depicts the surface interaction between the S peptide and S protein fragments; S peptide is blue, S protein is yellow. | ||
| source = | | source = | ||
| width =10 | | width =10 |