Sandbox Reserved 350: Difference between revisions

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'''(3)''' [(Fig. 5a.)]–A (P<sub>ʟ</sub>S) molecule occupies the opened specificity pocket.
'''(3)''' [(Fig. 5a.)]–A (P<sub>ʟ</sub>S) molecule occupies the opened specificity pocket.
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'''(4)''' Now the unfolded hydrophobic spikes, perforate the polar membrane surface; trp26, Trp27 and Leu79 side are immersed into the apolar core.
'''(4)''' Now the unfolded hydrophobic spikes, perforate the polar membrane surface; Trp26, Trp27 and Leu79 side are immersed into the apolar core.
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'''(5)''' Bottom of β-Barrel contacts negatively charged phosphate head groups on the membrane through favourable ionic interactions with basic residues located in the spikes and neighboring loops. <ref name="Lipid-protein blood interaction ">PMID: 9805008 </ref> <ref name="Prothrobins and lipids ">PMID: 2261453 </ref>
'''(5)''' Bottom of β-Barrel contacts negatively charged phosphate head groups on the membrane through favourable ionic interactions with basic residues located in the spikes and neighboring loops. <ref name="Lipid-protein blood interaction ">PMID: 9805008 </ref> <ref name="Prothrobins and lipids ">PMID: 2261453 </ref>
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=Finer Crystallography Details=
=Finer Crystallography Details=
''X-Ray Diffraction of the C2 Domain of Human Coagulation Factor V (1czv)'' <ref name="Pubmed"/>
''X-Ray Diffraction of the C2 Domain of Human Coagulation Factor V (1czv)'' <ref name="Pubmed"/>