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

<scene name='Studio:G4SecL04/A1_with_pointer/1'>α1</scene> (residues 38-76) and  

<scene name='Studio:G4SecL04/A5_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_2/1'>α2 (residues 95-112)</scene>,  

<scene name='Studio:G4SecL04/Alpha_2_and3/1' >α3 (residues 121-145)</scene>,  including a short  

<scene name='Studio:G4SecL04/Alpha_2_and3_and_4/1'>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/Beta_01/1' >β1 (residues 79-80)</scene>,and  

<scene name='Studio:G4SecL04/Beta_02/1' >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.