G1SecL05: Difference between revisions
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<Structure load='1fj1' size='600' frame='true' align='right' caption='3D Jmol model' | <Structure load='1fj1' size='600' frame='true' align='right' caption='3D Jmol model' | ||
scene='Insert optional scene name here' /> | scene='Insert optional scene name here' /> | ||
<scene name='G1SecL05/1fj1_chains_labeled/4'> | <scene name='G1SecL05/1fj1_chains_labeled/4'>Label All Chains</scene>--- | ||
<scene name='G1SecL05/1fj1-condensed/4'>Chain E</scene>---<scene name='G1SecL05/1fj1-condensed/3'>Close up view</scene> | <scene name='G1SecL05/1fj1-condensed/4'>Show Only Chain E</scene>---<scene name='G1SecL05/1fj1-condensed/3'>Close up view</scene> | ||
===Trp-216=== | ===Trp-216=== | ||
One hyper-variable region is the Tryptophan amino acid residue sequence 216. Polar amino acid side chains flank the Tryptophan, and changes in such amino acids can ultimately affect the reactivity of OspA to monoclonal antibodies. Differences in side chains of amino acids on the polar surface of a helical structure surrounding the highly conserved tryptophan residue 216 can affect the reactivity of OspA. | One hyper-variable region is the Tryptophan amino acid residue sequence 216. Polar amino acid side chains flank the Tryptophan, and changes in such amino acids can ultimately affect the reactivity of OspA to monoclonal antibodies. Differences in side chains of amino acids on the polar surface of a helical structure surrounding the highly conserved tryptophan residue 216 can affect the reactivity of OspA. | ||