Related ArticlesDynamic structure of the lower density lipoproteins. II. Deuterium NMR studies of the monolayer of very low and low density lipoproteins.
The order of phosphatidylcholine (PC) acyl chains in the surface monolayer of very low density lipoproteins (VLDL) and low density lipoproteins (LDL) has been determined from 2H nuclear magnetic resonance order parameters, SCD, using selectively deuterated PC or palmitic acids. From the computer simulated line shapes, we find two distinct phospholipid domains within the amphiphilic monolayer of both VLDL and LDL. In the more ordered domain of LDL, SCD was approximately 0.3 for the "plateau" chain region. The SCD values of VLDL particles are similar to those of LDL for the 5,6- and 11,12-positions, hence we suggest the organization of the more ordered region of VLDL and LDL are similar. The domain of low order in LDL comprises less than 10% of the phospholipid molecules (we do not distinguish between PC and sphingomyelin), having approximately the same order (SCD less than 0.1) as egg PC - sphingomyelin unilamellar vesicles. In VLDL, the domain of low order comprises between approximately 10 and approximately 20% of the phospholipid molecules and the entire acyl chain is in an essentially isotropic environment (SCD less than 0.02). We prepared VLDL-sized microemulsions composed of egg PC, deuterated PC, and triolein to test whether the apoproteins were responsible for creating the two differently organized domains in VLDL and LDL. Surprisingly, these protein-free particles also showed two domains of different order at two temperatures. The high order region, however, is less ordered than in VLDL and LDL. We explain two surface domains of PC in terms of lipid organization and the unique interactions of lipids in the various lipoprotein particles.
Molecular Hydrogen Tweezers: Structure and Mechanisms by Neutron Diffraction, NMR, and Deuterium Labeling Studies in Solid and Solution
Molecular Hydrogen Tweezers: Structure and Mechanisms by Neutron Diffraction, NMR, and Deuterium Labeling Studies in Solid and Solution
Felix Schulz, Victor Sumerin, Sami Heikkinen, Bjo?rn Pedersen, Cong Wang, Michiko Atsumi, Markku Leskela?, Timo Repo, Pekka Pyykko?, Winfried Petry and Bernhard Rieger
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja206394w/aop/images/medium/ja-2011-06394w_0015.gif
Journal of the American Chemical Society
DOI: 10.1021/ja206394w
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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11-30-2011 09:37 AM
[Question from NMRWiki Q&A forum] Might anyone donate a lower end NMR instrument?
Might anyone donate a lower end NMR instrument?
Hello, I am working in this really small university and things would be so better if we had a 60 or 90 MHz. I was wondering if any of you would know any means by which we could acquire one. May be there would be some organization that is willing to donate a functional one because they are upgrading. or may be some other reason. If I want to find out if anyone is donating an NMR where should I go. Are there any other such venues? thank you
Check if somebody has answered this question on NMRWiki QA forum
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01-20-2011 03:28 AM
[NMR paper] Deuterium NMR structure of retinal in the ground state of rhodopsin.
Deuterium NMR structure of retinal in the ground state of rhodopsin.
Related Articles Deuterium NMR structure of retinal in the ground state of rhodopsin.
Biochemistry. 2004 Oct 12;43(40):12819-28
Authors: Salgado GF, Struts AV, Tanaka K, Fujioka N, Nakanishi K, Brown MF
The conformation of retinal bound to the G protein-coupled receptor rhodopsin is intimately linked to its photochemistry, which initiates the visual process. Site-directed deuterium ((2)H) NMR spectroscopy was used to investigate the structure of retinal within the binding...
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11-24-2010 10:01 PM
[NMR paper] NMR solution structure of complement-like repeat CR3 from the low density lipoprotein
NMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein. Evidence for specific binding to the receptor binding domain of human alpha(2)-macroglobulin.
Related Articles NMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein. Evidence for specific binding to the receptor binding domain of human alpha(2)-macroglobulin.
J Biol Chem. 2000 Feb 4;275(5):3264-9
Authors: Dolmer K, Huang W, Gettins PG
We have used NMR methods to determine the...
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11-18-2010 09:15 PM
Cu and Fe metallic ions-mediated oxidation of low-density lipoproteins studied by NMR
Cu and Fe metallic ions-mediated oxidation of low-density lipoproteins studied by NMR, TEM and Z-scan technique.
Related Articles Cu and Fe metallic ions-mediated oxidation of low-density lipoproteins studied by NMR, TEM and Z-scan technique.
Chem Phys Lipids. 2010 Jun;163(6):545-51
Authors: Gómez SL, Monteiro AM, Rabbani SR, Bloise AC, Carneiro SM, Alves S, Gidlund M, Abdalla DS, Neto AM
In this work we report on a study of the morphological changes of LDL induced in vitro by metallic ions (Cu(2+) and Fe(3+)). These modifications were...
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10-22-2010 06:02 AM
[NMR paper] Structure and dynamic studies by NMR of the potent sweet protein monellin and a non-s
Structure and dynamic studies by NMR of the potent sweet protein monellin and a non-sweet analog. Evidence on the importance of residue AspB7 for sweet taste.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structure and dynamic studies by NMR of the potent sweet protein monellin and a non-sweet analog. Evidence on the importance of residue AspB7 for sweet taste.
FEBS Lett. 1997 Aug 25;413(3):409-16
Authors: Mizukoshi T, Kohmura M, Suzuki E, Ariyoshi Y
Monellin, an...
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08-22-2010 05:08 PM
[NMR paper] 1H NMR-based absolute quantitation of human lipoproteins and their lipid contents dir
1H NMR-based absolute quantitation of human lipoproteins and their lipid contents directly from plasma.
Related Articles 1H NMR-based absolute quantitation of human lipoproteins and their lipid contents directly from plasma.
J Lipid Res. 1994 Dec;35(12):2292-304
Authors: Ala-Korpela M, Korhonen A, Keisala J, Hörkkö S, Korpi P, Ingman LP, Jokisaari J, Savolainen MJ, Kesäniemi YA
A new method is presented for absolute quantitation of lipid and protein contents of human lipoproteins directly from plasma. The method enables complete lipoprotein...
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08-22-2010 03:29 AM
[NMR paper] NMR solution structure of complement-like repeat CR8 from the low density lipoprotein
NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein.
J Biol Chem. 1999 May 14;274(20):14130-6
Authors: Huang W, Dolmer K, Gettins PG
The low density lipoprotein receptor-related protein is a member of the low density...