Sandbox Reserved 1759: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains with what appears to be a 60% alpha helixes (pink) and 40% beta sheets (yellow) when viewing the <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The two subunits are homodimers, containing 9 alpha helix and 15 beta sheets each. The alpha helixes and beta sheets loop and fold to form a <scene name='93/934003/Tertiary_structure/1'>3D globular protein</scene>. The <scene name='93/934003/Space_filling/1'>space filling</scene> model helps to highlight the globular nature of the protein. Amphipathic.....In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well
The Protein is composed of alpha helix, beta sheet, and random coils. The protein consists of two major domains with what appears to be a 60% alpha helixes (pink) and 40% beta sheets (yellow) when viewing the <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The two subunits are homodimers, containing 9 alpha helix and 15 beta sheets each. The alpha helixes and beta sheets loop and fold to form a <scene name='93/934003/Tertiary_structure/1'>3D globular protein</scene>. The <scene name='93/934003/Space_filling/1'>space filling</scene> model helps to highlight the globular nature of the protein. Amphipathic.....In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well


</StructureSection>
</StructureSection>