G3p: Difference between revisions
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They used NMR spectroscopy to create a structure of the first domains of g3p. Shown is a combination of the 15 most energetically favorable states. Observations of secondary structure are below. | They used NMR spectroscopy to create a structure of the first domains of g3p. Shown is a combination of the 15 most energetically favorable states. Observations of secondary structure are below. | ||
<applet load='1g3p' size='200' frame='true' align=' | <applet load='1g3p' size='200' frame='true' align='right' caption='D1 and D2 domains of g3p' /> | ||
In 1998, Lubkowski et al crystallized the first two domains of g3p. They made two overall observations: | In 1998, Lubkowski et al crystallized the first two domains of g3p. They made two overall observations: | ||
(1) <scene name='G3p/Pro_213_in_cis_conformation/1'>Cis proline near C terminal end</scene> <ref name="lubkowski"/> and (2) <scene name='G3p/Oxidized_tryptophan/1'>An oxidized tryptophan</scene> <ref name="lubkowski"/>. The cis proline identified will later turn out to be important for function of the protein. The oxidized tryptophan, however, was not found in other structures <ref name="holliger 99"> PMID:10329170 </ref>. | (1) <scene name='G3p/Pro_213_in_cis_conformation/1'>Cis proline near C terminal end</scene> <ref name="lubkowski"/> and (2) <scene name='G3p/Oxidized_tryptophan/1'>An oxidized tryptophan</scene> <ref name="lubkowski"/>. The cis proline identified will later turn out to be important for function of the protein. The oxidized tryptophan, however, was not found in other structures <ref name="holliger 99"> PMID:10329170 </ref>. | ||
