User:Marvin O'Neal/OspC: Difference between revisions
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<scene name='Studio:G4SecL04/Random_coils/2' target='1'>random coils</scene> | <scene name='Studio:G4SecL04/Random_coils/2' target='1'>random coils</scene> | ||
. The N and C termini at the membrane proximal end of two long alpha helices, | . The N and C termini at the membrane proximal end of two long alpha helices, | ||
<scene name='Studio:G4SecL04/N_and_c_termini_with_helix/1' target='1'>α1 (residues 38-76) and α5 (residues 170-201)</scene> are in close proximity to each other. At the membrane distal end, there are three remaining alpha helices, α2 (residues ), α3 (residues) , including a short α4 (residues). At the end of membrane surface, the connection between helices α1 and α2 forms two short anti-parallel β-strands, β1 (residues 79-80) and β2 (residues 88-89) are formed. | <scene name='Studio:G4SecL04/N_and_c_termini_with_helix/1' target='1'>α1 (residues 38-76) and α5 (residues 170-201)</scene> are in close proximity to each other. At the membrane distal end, there are three remaining alpha helices, | ||
<scene name='Studio:G4SecL04/Alpha_2/1' target='1'>α2 (residues 95-112)</scene>, | |||
<scene name='Studio:G4SecL04/Alpha_2_and3/1' target='1'>α3 (residues 121-145)</scene>, including a short | |||
<scene name='Studio:G4SecL04/Alpha_2_and3_and_4/1' target='1'>α4 (residues 152-159)</scene>. At the end of membrane surface, the connection between helices α1 and α2 forms two short anti-parallel β-strands, β1 (residues 79-80) and β2 (residues 88-89) are formed. | |||
Based on the alignment of all oMGs, towards the membrane proximal end, the surface-exposed residues on α1 and α5 are highly conserved, resulting positively charged surface. Other than those on helices, α1 and α5, the surface-exposed residues on the remaining regions of OspC molecule are variable. | Based on the alignment of all oMGs, towards the membrane proximal end, the surface-exposed residues on α1 and α5 are highly conserved, resulting positively charged surface. Other than those on helices, α1 and α5, the surface-exposed residues on the remaining regions of OspC molecule are variable. | ||
