Related ArticlesInfluence of annexin V on the structure and dynamics of phosphatidylcholine/phosphatidylserine bilayers: a fluorescence and NMR study.
Biochemistry. 1998 Feb 3;37(5):1403-10
Authors: Saurel O, Cézanne L, Milon A, Tocanne JF, Demange P
The consequences of the binding of annexin V on the structure and dynamics of PC/PS bilayers were studied by means of fluorescence polarization, 31P NMR, 2H NMR, and fluorescence recovery after photobleaching (FRAP). Even at complete coverage of the lipid bilayers by the protein, annexin V showed no influence on the lipid molecular packing and the acyl chain flexibility of both PC and PS. The fluorescence polarization of the probe DPH, the 31P NMR spectra, and deuterium quadrupolar splittings of P(d31)OPS remained unchanged. However, upon binding of annexin V, two distinct populations of PC were visible in 2H NMR, which were in slow exchange on the deuterium NMR time scale (microseconds). One component in the spectrum was identical to the protein-free sample, while a second, broad, component appeared. The presence of the protein induced a decrease in the transverse relaxation times (T2e), indicative of the appearance of slow motions (milliseconds to microseconds), in the P(d31)-OPS spectrum and in the P(d31)OPC broad component. FRAP experiments were carried out with the probes C12-NBD-PC and C12-NBD-PS: at saturation, annexin V reduced the lateral diffusion rate of PC by 40% and nearly blocked the diffusion of PS. These combined experiments are consistent with a model in which annexin V enters a proteolipidic complex in the form of an extended 2D network, stabilized by specific interactions with PS. As seen from the lateral diffusion rates and the acyl chains NMR spectral parameters, two separate lipid populations appear, presumably corresponding to those interacting with annexinV (PC and PS) and protein free domains (mainly PC).
[NMR paper] Influence of chemical shift tolerances on NMR structure calculations using ARIA proto
Influence of chemical shift tolerances on NMR structure calculations using ARIA protocols for assigning NOE data.
Related Articles Influence of chemical shift tolerances on NMR structure calculations using ARIA protocols for assigning NOE data.
J Biomol NMR. 2005 Jan;31(1):21-34
Authors: Fossi M, Linge J, Labudde D, Leitner D, Nilges M, Oschkinat H
Large-scale protein structure determination by NMR via automatic assignment of NOESY spectra requires the adjustment of several parameters for optimal performance. Among those are the chemical shift...
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[NMR paper] Influence of pH on NMR structure and stability of the human prion protein globular do
Influence of pH on NMR structure and stability of the human prion protein globular domain.
Related Articles Influence of pH on NMR structure and stability of the human prion protein globular domain.
J Biol Chem. 2003 Sep 12;278(37):35592-6
Authors: Calzolai L, Zahn R
The NMR structure of the globular domain of the human prion protein (hPrP) with residues 121-230 at pH 7.0 shows the same global fold as the previously published structure determined at pH 4.5. It contains three alpha-helices, comprising residues 144-156, 174-194, and 200-228, and...
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[NMR paper] Influence of internal dynamics on accuracy of protein NMR structures: derivation of r
Influence of internal dynamics on accuracy of protein NMR structures: derivation of realistic model distance data from a long molecular dynamics trajectory.
Related Articles Influence of internal dynamics on accuracy of protein NMR structures: derivation of realistic model distance data from a long molecular dynamics trajectory.
J Mol Biol. 1999 Jan 15;285(2):727-40
Authors: Schneider TR, Brünger AT, Nilges M
In order to study the effect of internal dynamics on the accuracy of NMR structures in detail, we generated NOE distance data from a...
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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] Cardiotoxin II segregates phosphatidylglycerol from mixtures with phosphatidylcholine
Cardiotoxin II segregates phosphatidylglycerol from mixtures with phosphatidylcholine: (31)P and (2)H NMR spectroscopic evidence.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Cardiotoxin II segregates phosphatidylglycerol from mixtures with phosphatidylcholine: (31)P and (2)H NMR spectroscopic evidence.
Biochemistry. 1996 Mar 19;35(11):3368-78
Authors: Carbone MA, Macdonald PM
The interaction of the cationic protein cardiotoxin II (CTX II) with mixtures of zwitterionic...
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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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[NMR paper] Annexin V binding to the outer leaflet of small unilamellar vesicles leads to altered
Annexin V binding to the outer leaflet of small unilamellar vesicles leads to altered inner-leaflet properties: 31P- and 1H-NMR studies.
Related Articles Annexin 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...
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[NMR paper] NMR studies of phospholipase C hydrolysis of phosphatidylcholine in model membranes.
NMR studies of phospholipase C hydrolysis of phosphatidylcholine in model membranes.
Related Articles NMR studies of phospholipase C hydrolysis of phosphatidylcholine in model membranes.
J Biol Chem. 1993 Feb 5;268(4):2431-4
Authors: Bhamidipati SP, Hamilton JA
Hydrolysis of phospholipids in biological membranes by phospholipase C (PLC) produces an important second messenger molecule, 1,2-diacylglycerol (DAG), that is essential for the activation of protein kinase C (PKC). While the effects of DAG on model membranes have been investigated...
Influence of annexin V on the structure and dynamics of phosphatidylcholine/phosphati
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