User:Marvin O'Neal/OspC: Difference between revisions

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Irene Chen (talk | contribs)
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<scene name='Studio:G4SecL04/Alpha_1_with_pointer/1'>α1</scene> (residues 38-76) and  
<scene name='Studio:G4SecL04/Alpha_1_with_pointer/1'>α1</scene> (residues 38-76) and  
<scene name='Studio:G4SecL04/Alpha_5_with_pointer/1'>α5</scene> (residues 170-201) are in close proximity to each other.  At the membrane distal end, there are three remaining alpha helices,  
<scene name='Studio:G4SecL04/Alpha_5_with_pointer/1'>α5</scene> (residues 170-201) are in close proximity to each other.  At the membrane distal end, there are three remaining alpha helices,  
<scene name='Studio:G4SecL04/Alpha_2_with_pointer/1'>α2 (residues 95-112)</scene>,  
<scene name='Studio:G4SecL04/Alpha_2_with_pointer/1'>α2</scene> (residues 95-112),  
<scene name='Studio:G4SecL04/Alpha_3_with_pointer/1'>α3 (residues 121-145)</scene>, including a short  
<scene name='Studio:G4SecL04/Alpha_3_with_pointer/1'>α3</scene> (residues 121-145), including a short  
<scene name='Studio:G4SecL04/Alpha_4_with_pointer/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,  
<scene name='Studio:G4SecL04/Alpha_4_with_pointer/1'>α4</scene> (residues 152-159). At the end of membrane surface, the connection between helices α1 and α2 forms two short anti-parallel β-strands,  
<scene name='Studio:G4SecL04/Beta_1_with_pointer/2'>β1 (residues 79-80)</scene>,and  
<scene name='Studio:G4SecL04/Beta_1_with_pointer/2'>β1</scene> (residues 79-80),and  
<scene name='Studio:G4SecL04/Beta_2_with_pointer/1'>β2 (residues 88-89)</scene> 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.
<scene name='Studio:G4SecL04/Beta_2_with_pointer/1'>β2</scene> (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.


==Evolutionary Conservation of OspC==
==Evolutionary Conservation of OspC==
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