GLP-1: Difference between revisions
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Bound to the GLP-1 receptor, GLP-1 has an <scene name='10/1067195/Glp1_only/1'>alpha-helical structure</scene> that is <scene name='10/1067195/Cv1/1'>bent</scene> near glycine in some complexes. In solution, GLP-1 is <scene name='10/1067195/Glp-1_solution/1'>alpha-helical in its center</scene> according to NMR data. Looking at the helix-propensity of the peptide sequence, the N-terminal part of Glp-1 (7-37) is less likely to be alpha-helical than the C-terminal half. | Bound to the GLP-1 receptor, GLP-1 has an <scene name='10/1067195/Glp1_only/1'>alpha-helical structure</scene> that is <scene name='10/1067195/Cv1/1'>bent</scene> near glycine in some complexes. In solution, GLP-1 is <scene name='10/1067195/Glp-1_solution/1'>alpha-helical in its center</scene> according to NMR data. Looking at the helix-propensity of the peptide sequence, the N-terminal part of Glp-1 (7-37) is less likely to be alpha-helical than the C-terminal half. | ||
[[Image:GLP1 helix propensity.PNG | [[Image:GLP1 helix propensity.PNG]] | ||
== Synthesis through proglucagon processing== | == Synthesis through proglucagon processing== | ||
