Sandbox 35: Difference between revisions
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The <scene name='Sandbox_35/Secondary_structure_colored/1'>secondary structure</scene> of Adenylate Kinase has alpha helicies (purple) and beta sheets (dark pink) that circle around and enclose the non-hydrolysable part of the protein (seen in the center). | The <scene name='Sandbox_35/Secondary_structure_colored/1'>secondary structure</scene> of Adenylate Kinase has alpha helicies (purple) and beta sheets (dark pink) that circle around and enclose the non-hydrolysable part of the protein (seen in the center). | ||
One of the main components of protein structure are the <scene name='Sandbox_35/Secondary_h_bonds2/1'>hydrogen bonds</scene> which are shown in green on this structure. The hydrogen bonds form links between adjacent amino acids, contributing to the protein structure and fold. The hydrogen bonds on the beta sheets are in an anti-parallel configuration, which offers stability for the protein. | One of the main components of protein structure are the <scene name='Sandbox_35/Secondary_h_bonds2/1'>hydrogen bonds</scene> which are shown in green on this structure. The hydrogen bonds form links between adjacent amino acids, contributing to the protein structure and fold. The hydrogen bonds on the beta sheets are in an anti-parallel configuration, which offers stability for the protein. | ||
==Hydrophobic and Hydrophilic Residue Composition== | |||
Adenylate kinase is composed of both hydrophobic and hydrophilic residues, and folds accordingly to obtain the optimum environments for the nature of both kinds of residues. The <scene name='Sandbox_35/Secondary_hydrophobs_only_gre/1'>hydrophobic residues</scene> shown in grey are buried within the folded protein, away from contact with the solvent. This action represents the hydrophobic effect taking place, which is mainly driven by entropy. | |||
