Sandbox Reserved 1456: Difference between revisions

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The main <scene name='79/799584/Secondary_structure/1'>secondary structures</scene> present in Kgp are alpha helices and antiparallel beta sheets. Alpha helices and beta sheets impact how the protein will fold by allowing for specific amino acid interactions. Alpha helices are tightly wound with a center channel too small for even a hydrogen atom to pass through. Alpha helices and beta sheets cannot have a glycine or proline residue as part of the chain and are only found in beta-turns. By knowing this, you know that glycine and proline would not be found in the primary amino acid sequence where the alpha helices and beta sheets would be found.  
The main <scene name='79/799584/Secondary_structure/1'>secondary structures</scene> present in Kgp are alpha helices and antiparallel beta sheets. Alpha helices and beta sheets impact how the protein will fold by allowing for specific amino acid interactions. Alpha helices are tightly wound with a center channel too small for even a hydrogen atom to pass through. Alpha helices and beta sheets cannot have a glycine or proline residue as part of the chain and are only found in beta-turns. By knowing this, you know that glycine and proline would not be found in the primary amino acid sequence where the alpha helices and beta sheets would be found.  


This <scene name='79/799584/Spacefill_rainbow/1'>space-fill</scene> model shows that the atoms that make up Kgp do not leave much room for other molecules to pass through. The <scene name='79/799584/Spacefill_hydrophobicity_2/1'>hydrophobicity-focused view</scene> of the surface of Kgp shows a fairly even distribution of hydrophobic (gray) and hydrophilic (purple) atoms. The red atoms are the solvent, and they are interacting with the hydrophilic atoms present on the surface of Kgp.  
This <scene name='79/799584/Spacefill_rainbow_2/1'>space-fill model</scene> shows that the atoms that make up Kgp do not leave much room for other molecules to pass through. The <scene name='79/799584/Spacefill_hydrophobicity_2/1'>hydrophobicity-focused view</scene> of the surface of Kgp shows a fairly even distribution of hydrophobic (gray) and hydrophilic (purple) atoms. The red atoms are the solvent, and they are interacting with the hydrophilic atoms present on the surface of Kgp.  




Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Emily Albertsen