1dep: Difference between revisions
New page: left|200px<br /><applet load="1dep" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dep" /> '''MEMBRANE PROTEIN, NMR, 1 STRUCTURE'''<br /> ... |
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[[Image:1dep.gif|left|200px]]<br /><applet load="1dep" size=" | [[Image:1dep.gif|left|200px]]<br /><applet load="1dep" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''MEMBRANE PROTEIN, NMR, 1 STRUCTURE'''<br /> | '''MEMBRANE PROTEIN, NMR, 1 STRUCTURE'''<br /> | ||
==Overview== | ==Overview== | ||
The C-terminal part of the third intracellular loop of the | The C-terminal part of the third intracellular loop of the beta-adrenoceptor is capable of stimulating adenylate cyclase in the presence of phospholipid vesicles via the stimulatory guanine nucleotide binding protein (Gs) [Palm et al. (1989) FEBS Lett. 254, 89-93]. We have investigated the structure of synthetic peptides corresponding to residues 284-295 of the turkey erythrocyte adrenoceptor in micelles, trifluoroethanol and aqueous solution, by using 2D 1H NMR and CD. In the presence of phospholipid micelles the peptides display a C-terminal alpha-helical region, whereas the N-terminal part was found to be highly flexible. | ||
==About this Structure== | ==About this Structure== | ||
1DEP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http:// | 1DEP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DEP OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Jung, H.]] | [[Category: Jung, H.]] | ||
[[Category: Schnackerz, K | [[Category: Schnackerz, K D.]] | ||
[[Category: beta-adrenoceptor]] | [[Category: beta-adrenoceptor]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
[[Category: micelle-bound peptide]] | [[Category: micelle-bound peptide]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:55 2008'' | ||
Revision as of 13:15, 21 February 2008
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MEMBRANE PROTEIN, NMR, 1 STRUCTURE
OverviewOverview
The C-terminal part of the third intracellular loop of the beta-adrenoceptor is capable of stimulating adenylate cyclase in the presence of phospholipid vesicles via the stimulatory guanine nucleotide binding protein (Gs) [Palm et al. (1989) FEBS Lett. 254, 89-93]. We have investigated the structure of synthetic peptides corresponding to residues 284-295 of the turkey erythrocyte adrenoceptor in micelles, trifluoroethanol and aqueous solution, by using 2D 1H NMR and CD. In the presence of phospholipid micelles the peptides display a C-terminal alpha-helical region, whereas the N-terminal part was found to be highly flexible.
About this StructureAbout this Structure
1DEP is a Single protein structure of sequence from Meleagris gallopavo. Full crystallographic information is available from OCA.
ReferenceReference
NMR and circular dichroism studies of synthetic peptides derived from the third intracellular loop of the beta-adrenoceptor., Jung H, Windhaber R, Palm D, Schnackerz KD, FEBS Lett. 1995 Jan 23;358(2):133-6. PMID:7828722
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