Bucandin: Difference between revisions

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The amino acid tryptophan has an aromatic hydrophobic side chain. These side chains, Trp27 and Trp36 are facing towards the tip of the middle loop of the amino acid residues, giving the molecule as a whole a little bit of flexibility, showing us that Bucandin is not rigid.

The structure was also solved through crystallography. An electron density map is used to model X-ray structure determination. In X-ray structure determination, we shoot X-rays at a crystal structure of a protein and catch the refracted rays on a film. This allows us to create the pattern which in turn gives us the X-rays along with the intensity of the X-rays that gives us the final structure of the protein. The electron density map of Bucandin gives us some insight into the structure of this protein. It shows how the different amino acids form peptide bonds and when their structures are oriented in a certain direction. For example, by using the electron density map, we can see that there is an asparagine attached to glutamate at one point in the structure. According to <ref name ='Kuhn et a.l'> PMID:11053837 </ref>, “the resulting electron density maps were of outstanding quality and allowed the automated tracing of 61 of 63 amino acid residues, including their side chains, and the placement of 48 solvent molecules”. This high-resolution structure allows us to obtain a greater understanding of the general structure and properties of Bucandin to identify specific characteristics of the protein.

The structure was also solved through crystallography. An electron density map <ref name = 'EDM'> electron </ref> is used to model X-ray structure determination. In X-ray structure determination, we shoot X-rays at a crystal structure of a protein and catch the refracted rays on a film. This allows us to create the pattern which in turn gives us the X-rays along with the intensity of the X-rays that gives us the final structure of the protein. The electron density map of Bucandin gives us some insight into the structure of this protein. It shows how the different amino acids form peptide bonds and when their structures are oriented in a certain direction. For example, by using the electron density map, we can see that there is an asparagine attached to glutamate at one point in the structure. According to <ref name ='Kuhn et a.l'> PMID:11053837 </ref>, “the resulting electron density maps were of outstanding quality and allowed the automated tracing of 61 of 63 amino acid residues, including their side chains, and the placement of 48 solvent molecules”. This high-resolution structure allows us to obtain a greater understanding of the general structure and properties of Bucandin to identify specific characteristics of the protein.

</StructureSection>

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@@ Line 16: / Line 16: @@
 The amino acid tryptophan has an aromatic hydrophobic side chain. These side chains, Trp27 and Trp36 are facing towards the tip of the middle loop of the amino acid residues, giving the molecule as a whole a little bit of flexibility, showing us that Bucandin is not rigid.
-The structure was also solved through crystallography. An electron density map is used to model X-ray structure determination. In X-ray structure determination, we shoot X-rays at a crystal structure of a protein and catch the refracted rays on a film. This allows us to create the pattern which in turn gives us the X-rays along with the intensity of the X-rays that gives us the final structure of the protein. The electron density map of Bucandin gives us some insight into the structure of this protein. It shows how the different amino acids form peptide bonds and when their structures are oriented in a certain direction. For example, by using the electron density map, we can see that there is an asparagine attached to glutamate at one point in the structure. According to <ref name ='Kuhn et a.l'> PMID:11053837 </ref>, “the resulting electron density maps were of outstanding quality and allowed the automated tracing of 61 of 63 amino acid residues, including their side chains, and the placement of 48 solvent molecules”. This high-resolution structure allows us to obtain a greater understanding of the general structure and properties of Bucandin to identify specific characteristics of the protein.
+The structure was also solved through crystallography. An electron density map <ref name = 'EDM'> electron </ref> is used to model X-ray structure determination. In X-ray structure determination, we shoot X-rays at a crystal structure of a protein and catch the refracted rays on a film. This allows us to create the pattern which in turn gives us the X-rays along with the intensity of the X-rays that gives us the final structure of the protein. The electron density map of Bucandin gives us some insight into the structure of this protein. It shows how the different amino acids form peptide bonds and when their structures are oriented in a certain direction. For example, by using the electron density map, we can see that there is an asparagine attached to glutamate at one point in the structure. According to <ref name ='Kuhn et a.l'> PMID:11053837 </ref>, “the resulting electron density maps were of outstanding quality and allowed the automated tracing of 61 of 63 amino acid residues, including their side chains, and the placement of 48 solvent molecules”. This high-resolution structure allows us to obtain a greater understanding of the general structure and properties of Bucandin to identify specific characteristics of the protein.
 </StructureSection>
 == References ==
 <references/>