G18secL03Tpc4: Difference between revisions

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 OspC is predominantly <scene name='G18secL03Tpc4/Alpha_helix_highlighted/1'>α-helical</scene> in its secondary structure. <scene name='G18secL03Tpc4/Beta_sheets/1'>β-sheets</scene> are also present, but they are rather short and not promininent. OspC is unique when compared to its sister proteins, OspA and OspB, which are made up of beta-sheets mostly.<ref>D.Brisson, D.E Dykhuizen. OspC diversity in Borrelia burgdorferi: Different Hosts are Different Niches. Genetics 2004 October; Volume 168 (2): 713-722. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1448846/]</ref>
 *Tertiary Structure
-A single OspC monomer subunit is composed of 4 long and 1 short α-helices. Also, 2 short segments of β-sheets are observed near the binding site of the molecule.
+A single OspC monomer subunit is composed of 4 long and 1 short α-helices. Also, 2 short segments of β-sheets are observed near the binding site of the molecule. The molecule also contains six <scene name='G18secL03Tpc4/Random_coils/1'>random coils</scene> throughout the structure on each subunit.
 *Quaternary Structure
 OspC is a dimerized molecule, with 2 identical monomeric subunits comprising a dimer. However, for a binding event to occur, a tetramer made up of two dimers is necessary.