NitroDur: Difference between revisions
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<scene name='74/745476/Cys-302_of_aldh2/1'></scene> | <scene name='74/745476/Cys-302_of_aldh2/1'></scene> | ||
<StructureSection load='' size='340' side='right' caption='Human aldehyde dehydrogenase complex with nitroglycerin (PDB code [[4fr8]])' scene='74/745476/Humanaldehydedehydrogenase/1'> | <StructureSection load='4fr8.pdb' size='340' side='right' caption='Human aldehyde dehydrogenase complex with nitroglycerin (PDB code [[4fr8]])' scene='74/745476/Humanaldehydedehydrogenase/1'> | ||
==Structure== | ==Structure== | ||
The main ingredient of NitroDur is 1,2,3-propanetriol trinitrate, also known as <scene name='74/745476/Nitroglycerinmolecule/3'>Nitroglycerin</scene>. '''Nitroglycerin''' is a molecule that when broken down to nitric oxide binds to protein domains found in smooth muscle. These binding domains are often found in the form of dimers that require multiple NO molecules to bind as seen in <scene name='74/745476/2o0c_molecule/3'>Nitric Oxide bound to the domain of Nostoc cyanbacterial protein</scene>. Nitric Oxide is often buried deep within the protein, that in conjunction with other molecular interactions, triggers structural changes that activate proteins to serve their specific functions. In humans, NO binds to protein domains in this same fashion, as seen in <scene name='74/745476/Guanylate_cyclase/2'>Heterodimeric Catalytic Domain of Wild-type Human Soluble Guanylate Cyclase </scene>. | The main ingredient of NitroDur is 1,2,3-propanetriol trinitrate, also known as <scene name='74/745476/Nitroglycerinmolecule/3'>Nitroglycerin</scene>. '''Nitroglycerin''' is a molecule that when broken down to nitric oxide binds to protein domains found in smooth muscle. These binding domains are often found in the form of dimers that require multiple NO molecules to bind as seen in <scene name='74/745476/2o0c_molecule/3'>Nitric Oxide bound to the domain of Nostoc cyanbacterial protein</scene>. Nitric Oxide is often buried deep within the protein, that in conjunction with other molecular interactions, triggers structural changes that activate proteins to serve their specific functions. In humans, NO binds to protein domains in this same fashion, as seen in <scene name='74/745476/Guanylate_cyclase/2'>Heterodimeric Catalytic Domain of Wild-type Human Soluble Guanylate Cyclase </scene>. | ||
