1i5j
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1i5j.gif|left|200px]] | [[Image:1i5j.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1i5j", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1i5j| PDB=1i5j | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS''' | '''NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS''' | ||
| Line 29: | Line 26: | ||
[[Category: Howlett, G J.]] | [[Category: Howlett, G J.]] | ||
[[Category: MacRaild, C A.]] | [[Category: MacRaild, C A.]] | ||
| - | [[Category: | + | [[Category: Amphipathic alpha helix]] |
| - | [[Category: | + | [[Category: Protein-lipid interaction]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:35:59 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:36, 2 May 2008
NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS
Overview
The structure and protein-detergent interactions of apolipoprotein C-II (apoC-II) in the presence of SDS micelles have been investigated using circular dichroism and heteronuclear NMR techniques applied to (15)N-labeled protein. Micellar SDS, a commonly used mimetic of the lipoprotein surface, inhibits the aggregation of apoC-II and induces a stable structure containing approximately 60% alpha-helix as determined by circular dichroism. NMR reveals the first 12 residues of apoC-II to be structurally heterogeneous and largely disordered, with the rest of the protein forming a predominantly helical structure. Three regions of helical conformation, residues 16-36, 50-56, and 63-77, are well-defined by NMR-derived constraints, with the intervening regions showing more loosely defined helical conformation. The structure of apoC-II is compared to that determined for other apolipoproteins in a similar environment. Our results shed light on the lipid interactions of apoC-II and its mechanism of lipoprotein lipase activation.
About this Structure
1I5J is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate., MacRaild CA, Hatters DM, Howlett GJ, Gooley PR, Biochemistry. 2001 May 8;40(18):5414-21. PMID:11331005 Page seeded by OCA on Fri May 2 19:35:59 2008
