Related ArticlesNMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.
Biochemistry. 2001 May 8;40(18):5414-21
Authors: MacRaild CA, Hatters DM, Howlett GJ, Gooley PR
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.
13C-Labeled Heparan Sulfate Analogue as a Tool To Study Protein/Heparan Sulfate Interactions by NMR Spectroscopy: Application to the CXCL12? Chemokine
13C-Labeled Heparan Sulfate Analogue as a Tool To Study Protein/Heparan Sulfate Interactions by NMR Spectroscopy: Application to the CXCL12? Chemokine
Ce?dric Laguri, Nicolas Sapay, Jean-Pierre Simorre, Bernhard Brutscher, Anne Imberty, Pierre Gans and Hugues Lortat-Jacob
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja201753e/aop/images/medium/ja-2011-01753e_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja201753e
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interaction by NMR spectroscopy. Application to the CXCL12? chemokine.
13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interaction by NMR spectroscopy. Application to the CXCL12? chemokine.
13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interaction by NMR spectroscopy. Application to the CXCL12? chemokine.
J Am Chem Soc. 2011 Jun 2;
Authors: Laguri C, Sapay N, Simorre JP, Brutscher B, Imberty A, Gans P, Lortat-Jacob H
Heparan sulfate, a polysaccharide of the glycosaminoglycan family characterized by a unique level of complexity, has emerged as a key...
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06-04-2011 11:26 AM
Solution NMR Structure of apo-calmodulin in complex with the IQ motif of Human Cardiac Sodium Channel Na(V)1.5.
Solution NMR Structure of apo-calmodulin in complex with the IQ motif of Human Cardiac Sodium Channel Na(V)1.5.
Solution NMR Structure of apo-calmodulin in complex with the IQ motif of Human Cardiac Sodium Channel Na(V)1.5.
J Mol Biol. 2010 Dec 14;
Authors: Chagot B, Chazin WJ
The function of the human voltage-gated sodium channel Na(V)1.5 is regulated in part by intracellular calcium signals. The ubiquitous calcium sensor protein calmodulin (CaM) is an important part of the complex calcium-sensing apparatus in Na(V)1.5. CaM interacts with an IQ...
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12-21-2010 01:00 PM
[NMR paper] NMR solution structure and dynamics of an exchangeable apolipoprotein, Locusta migrat
NMR solution structure and dynamics of an exchangeable apolipoprotein, Locusta migratoria apolipophorin III.
Related Articles NMR solution structure and dynamics of an exchangeable apolipoprotein, Locusta migratoria apolipophorin III.
J Biol Chem. 2003 Jun 6;278(23):21212-20
Authors: Fan D, Zheng Y, Yang D, Wang J
We report here the NMR structure and backbone dynamics of an exchangeable apolipoprotein, apoLp-III, from the insect Locusta migratoria. The NMR structure adopts an up-and-down elongated five-helix bundle, which is similar to the...
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11-24-2010 09:01 PM
[NMR paper] NMR structure and dynamics of a receptor-active apolipoprotein E peptide.
NMR structure and dynamics of a receptor-active apolipoprotein E peptide.
Related Articles NMR structure and dynamics of a receptor-active apolipoprotein E peptide.
J Biol Chem. 2002 Aug 9;277(32):29172-80
Authors: Raussens V, Slupsky CM, Ryan RO, Sykes BD
Apolipoprotein E (apoE) is important in lipid metabolism due to its interaction with members of the low density lipoprotein (LDL) receptor family. ApoE is able to interact with the LDL receptor only when it is bound to lipid particles. To address structural aspects of this phenomenon, a...
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[NMR paper] The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR
The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy.
Biochemistry. 1997 Nov 4;36(44):13657-66
Authors: Wang G, Sparrow JT, Cushley RJ
The conformation of a synthetic peptide of 46 residues from apoA-I was investigated by fluorescence, CD, and 2D NMR spectroscopies in lipid-mimetic environments....
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08-22-2010 05:08 PM
[NMR paper] Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.
Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.
Related Articles Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.
Biochemistry. 1994 Nov 8;33(44):12990-7
Authors: Papavoine CH, Konings RN, Hilbers CW, van de Ven FJ
The major coat protein (gVIIIp) of bacteriophage M13 solubilized in sodium dodecyl sulfate (SDS) detergent micelles was used as a model system to study this protein in the lipid-bound form. In order to probe the position of gVIIIp relative to the SDS...
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[NMR paper] Interaction of apocytochrome c and derived polypeptide fragments with sodium dodecyl
Interaction of apocytochrome c and derived polypeptide fragments with sodium dodecyl sulfate micelles monitored by photochemically induced dynamic nuclear polarization 1H NMR and fluorescence spectroscopy.
Related Articles Interaction of apocytochrome c and derived polypeptide fragments with sodium dodecyl sulfate micelles monitored by photochemically induced dynamic nuclear polarization 1H NMR and fluorescence spectroscopy.
Biochemistry. 1991 Apr 9;30(14):3387-95
Authors: Snel MM, Kaptein R, de Kruijff B
The topology of apocytochrome c, the...