Sandbox Reserved 815: Difference between revisions
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The protein exists in majority in its dimer form. | The protein exists in majority in its dimer form. | ||
Between each <scene name='User:Erin_May/Sandbox_1/Nonpolar_at_dimer_interface/2'> helix 144-156</scene> of the two proteins, it exists many interactions whose stabilize the dimer interface. It can be retain acidic and mostly negative residues, or basic and positive residues. | Between each <scene name='User:Erin_May/Sandbox_1/Nonpolar_at_dimer_interface/2'> helix 144-156</scene> of the two proteins, it exists many interactions whose stabilize the dimer interface. It can be retain acidic and mostly negative residues, or basic and positive residues. | ||
Each is linked to the C-terminal <scene name='User:Erin_May/Sandbox_1/Helix_2_with_helix_3/1'> | Each is linked to the C-terminal <scene name='User:Erin_May/Sandbox_1/Helix_2_with_helix_3/1'> Helix 200-225</scene> of the other monomer. [http://en.wikipedia.org/wiki/Van_der_Waals_forces Van der Waals] forces are here between such nonpolar residues as valine, isoleucine, and nonpolar sections as histadine, methionine, and glutamic acid. | ||
It occurs hydrogen bonding between the dimers at <scene name='User:Erin_May/Sandbox_1/Interface_hydrogen_bonding/1'> Thr188 O−Gly195 N</scene>, Thr190 O−Lys194 N and Thr192 O−Thr192 N | It occurs hydrogen bonding between the dimers at <scene name='User:Erin_May/Sandbox_1/Interface_hydrogen_bonding/1'> Thr188 O−Gly195 N</scene>, Thr190 O−Lys194 N and Thr192 O−Thr192 N | ||
On each monomer, a Hydrogen bond between <scene name='User:Erin_May/Sandbox_1/Hydrogen_bond_asp_202/1'>Asp 202 and Thr 199</scene> stabilize the dimeric structure. | On each monomer, a Hydrogen bond between <scene name='User:Erin_May/Sandbox_1/Hydrogen_bond_asp_202/1'>Asp 202 and Thr 199</scene> stabilize the dimeric structure. | ||
