Related ArticlesAnnexin V binding to the outer leaflet of small unilamellar vesicles leads to altered inner-leaflet properties: 31P- and 1H-NMR studies.
Biochemistry. 1994 Sep 13;33(36):10944-50
Authors: Swairjo MA, Roberts MF, Campos MB, Dedman JR, Seaton BA
Calcium-dependent binding to phospholipid membranes is closely associated with annexin functional properties. In these studies, 31P- and 1H-nuclear magnetic resonance (NMR) experiments have been performed to study the effects of binding of recombinant rat annexin V to sonicated small unilamellar vesicles (SUVs). High-resolution 31P-NMR spectra of SUVs containing mixtures of synthetic phosphatidic acid (PA) and phosphatidylcholine (PC) show resolvable resonances corresponding to the inner-leaflet PA, outer-leaflet PA, and PC phosphoryl groups. When annexin binding occurs, the outer-leaflet PA 31P resonance shifts while that of PC is unaffected, consistent with selective binding of the protein to the phosphoryl moiety of the PA component. Further, annexin V binding to membrane outer-leaflet phospholipids has a measurable effect on inner-leaflet phospholipids of intact vesicles. 1H-NMR T1 relaxation measurements of SUVs containing acyl-chain-perdeuterated PC show no effects on the PA hydrocarbon-chain segmental motions upon annexin binding. Circular dichroism measurements indicate that the protein does not undergo a significant conformational change upon binding to the vesicles. The observed NMR changes do not correspond to proton or calcium gradients, nor to lateral segregation of extended patches of homogeneous phospholipids. The combined evidence suggests that selective, peripheral annexin-membrane interactions influence the environment of the inner vesicular surface. The mechanism proposed is a protein-induced change in vesicle morphology that corresponds to reduced curvature.
Understanding small-molecule binding to MDM2: insights into structural effects of isoindolinone inhibitors from NMR spectroscopy.
Understanding small-molecule binding to MDM2: insights into structural effects of isoindolinone inhibitors from NMR spectroscopy.
Understanding small-molecule binding to MDM2: insights into structural effects of isoindolinone inhibitors from NMR spectroscopy.
Chem Biol Drug Des. 2011 May;77(5):301-8
Authors: Riedinger C, Noble ME, Wright DJ, Mulks F, Hardcastle IR, Endicott JA, McDonnell JM
The interaction between murine double minute (MDM2) and p53 is a major target in anticancer drug design. Several potent compound series, including the nutlins...
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4,4'-Dithiobis-dipicolinic Acid: A Small and Convenient Lanthanide Binding Tag for Protein NMR Spectroscopy.
4,4'-Dithiobis-dipicolinic Acid: A Small and Convenient Lanthanide Binding Tag for Protein NMR Spectroscopy.
4,4'-Dithiobis-dipicolinic Acid: A Small and Convenient Lanthanide Binding Tag for Protein NMR Spectroscopy.
Chemistry. 2011 May 3;
Authors: Jia X, Maleckis A, Huber T, Otting G
Pseudocontact shifts (PCS) from paramagnetic lanthanide ions present powerful long-range structure restraints for studies of proteins by nuclear magnetic resonance spectroscopy. To elicit PCSs, the lanthanide must be attached site-specifically to the target protein....
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Small molecules against Ebola: NMR reveals drug leads
Small molecules against Ebola: NMR reveals drug leads
There is neither vaccine nor cure for the Ebola virus, which causes fatal haemorrhagic fever in humans. However, a new NMR spectroscopic study by US researchers scientists has led to the discovery of a family of small molecules that apparently bind to the outer protein coat of the virus and halt its entry into human cells, so offering the possibility of an antiviral medication against the disease.
Source: Spectroscopynow.com
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[NMR paper] NMR analyses of the interactions of human annexin I with ATP, Ca2+, and Mg2+.
NMR analyses of the interactions of human annexin I with ATP, Ca2+, and Mg2+.
Related Articles NMR analyses of the interactions of human annexin I with ATP, Ca2+, and Mg2+.
FEBS Lett. 1998 Apr 3;425(3):523-7
Authors: Han HY, Lee YH, Oh JY, Na DS, Lee BJ
Human annexin I is a member of the annexin family of calcium-dependent phospholipid binding proteins. The structure of an N-terminally truncated human annexin I (delta-annexin I) and its interactions with Ca2+, Mg2+, and ATP were studied at the atomic level using nuclear magnetic resonance...
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[NMR paper] Folding properties of an annexin I domain: a 1H-15N NMR and CD study.
Folding properties of an annexin I domain: a 1H-15N NMR and CD study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Folding properties of an annexin I domain: a 1H-15N NMR and CD study.
Biochemistry. 1996 Aug 13;35(32):10347-57
Authors: Cordier-Ochsenbein F, Guerois R, Baleux F, Huynh-Dinh T, Chaffotte A, Neumann JM, Sanson A
The annexin fold consists of four 70-residue domains with markedly homologous sequences and nearly identical structures. Each domain contains five helices...
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08-22-2010 02:20 PM
[NMR paper] Co2+ as a shift reagent for 35Cl NMR of chloride with vesicles and cells.
Co2+ as a shift reagent for 35Cl NMR of chloride with vesicles and cells.
Related Articles Co2+ as a shift reagent for 35Cl NMR of chloride with vesicles and cells.
Biochemistry. 1992 Jul 14;31(27):6272-8
Authors: Shachar-Hill Y, Shulman RG
Applications of high-resolution 35Cl NMR to the study of chloride in vivo and in vesicles have hitherto been limited by problems of NMR detectability and of resolving internal from external signals. We have characterized the effects of Co2+ on the 35Cl resonance of Cl- in solution and have shown that when...
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[NMR paper] Temperature-reversible eruptions of vesicles in model membranes studied by NMR.
Temperature-reversible eruptions of vesicles in model membranes studied by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Temperature-reversible eruptions of vesicles in model membranes studied by NMR.
Biophys J. 1992 May;61(5):1413-26
Authors: Nezil FA, Bayerl S, Bloom M
Deuterium (2H) and phosphorus (31P) nuclear magnetic resonance (NMR) and...
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[NMR paper] RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprote
RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins.
Proc Natl Acad Sci U S A. 1991 Mar 15;88(6):2495-9
Authors: Hoffman DW, Query CC, Golden BL, White...