Sandbox 51: Difference between revisions

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=== Secondary Structure ===
=== Secondary Structure ===


The structure of lysozyme with its <scene name='Sandbox_39/Secondary_structure/1'>Secondary Structure</scene> highlighted in yellow and pink can be seen to your left. The structures highlight the alpha helicies, and the yellow lines highlight the beta-pleated sheets. This depiction of Lysozyme contains six alpha helicies and three beta-pleated sheets, although the number of alpha helicies and beta pleated sheet in lysozyme can change depending on its structure in its original location. This depiction of lysozyme contains an antiparallel beta-pleated sheet, which contributes greatly to the stability of the molecule by providing the correct alignment of hydrogen bonds. Lysozyme also contains a great deal of random coil, which is seen in the white regions of the molecule.
Lysozyme contains five <scene name='Sandbox_38/A/2'>alpha helical</scene> regions and five regions containing <scene name='Sandbox_38/B/1'>beta sheets</scene> as displayed in this <scene name='Sandbox_38/Alphab/1'>image</scene>. Linking these secondary structures, a number of beta turns and large amount of random coil makes up the remainder of the polypeptide backbone. The polypeptide backbone of lysozyme involved in the 3 antiparallel beta sheets display the beta hairpin motif of supersecondary structure.This depiction of lysozyme contains an antiparallel beta-pleated sheet, which contributes greatly to the stability of the molecule by providing the correct alignment of hydrogen bonds. Lysozyme also contains a great deal of random coil, which is seen in the white regions of the molecule.




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