Related Articles2H-NMR investigation of DMPC/glycophorin bilayers.
Biochim Biophys Acta. 1994 Jul 13;1193(1):127-37
Authors: Shan X, Davis JH, Chu JW, Sharom FJ
Deuterium nuclear magnetic resonance spectroscopy was used to investigate the phase equilibria, and the temperature and concentration dependences of the phospholipid hydrocarbon chain order, of mixtures of glycophorin in dimyristoylphosphatidyl-choline. In the fluid phase it is found that the protein has only a slight effect on the first moment of the 2H spectrum, which for perdeuterated chains is a direct measure of the average chain orientational order. However, analysis of the rate of change of the first moment with respect to protein concentration, at different temperatures within the fluid phase, shows that at a molar protein concentration of about 0.0295 +/- 0.01, the lipid chain order (or M1) is essentially independent of temperature. At this concentration the chain order is determined by the lipid's interaction with the protein and one can conclude that about 34 (+/- 12) lipids are required to solvate the protein. At higher lipid concentrations these lipids are freely exchanging, on the NMR time scale, with the other lipids in the bilayer. At glycophorin concentrations below about 1 mol% there is a two-phase coexistence region at temperatures below the pure lipid's chain melting transition. The boundary between the fluid phase and this two-phase region curves downwards (is concave downwards), whereas the boundary between the two-phase region and the gel phase, while naturally occurring at lower temperatures than the upper boundary, is concave upwards. As a consequence the protein partitions preferentially into the fluid phase. This behaviour is similar to that observed in a number of other protein/lipid and peptide/lipid mixtures where it was suggested that those systems may have been close to a critical mixing point and some characteristics of a continuous phase change were noted. Indeed, at glycophorin concentrations near and above 1 mol% there are indications that the phase behaviour becomes more complex, suggesting the presence of significant protein/protein interactions and that this system may be close to a critical point.
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
J Am Chem Soc. 2011 Mar 14;
Authors: Yang J, Aslimovska L, Glaubitz C
Environmental factors such as temperature, hydration, and lipid bilayer properties are tightly coupled to the dynamics of membrane proteins. So far, site-resolved data visualizing the protein's response to alterations in these factors are rare, and conclusions had to be drawn from dynamic data averaged over the whole protein...
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[NMR paper] Investigation of the interaction of myelin basic protein with phospholipid bilayers u
Investigation of the interaction of myelin basic protein with phospholipid bilayers using solid-state NMR spectroscopy.
Related Articles Investigation of the interaction of myelin basic protein with phospholipid bilayers using solid-state NMR spectroscopy.
Chem Phys Lipids. 2004 Nov;132(1):47-54
Authors: Pointer-Keenan CD, Lee DK, Hallok K, Tan A, Zand R, Ramamoorthy A
Interaction of bovine myelin basic protein and its constituent charge isomers (C1-C3) with phospholipid bilayers was studied using solid-state NMR experiments on model...
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[NMR paper] Direct observation and characterization of DMPC/DHPC aggregates under conditions rele
Direct observation and characterization of DMPC/DHPC aggregates under conditions relevant for biological solution NMR.
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Biochim Biophys Acta. 2004 Aug 30;1664(2):241-56
Authors: van Dam L, Karlsson G, Edwards K
We have used cryo-transmission electron microscopy (cryo-TEM) for inspection of aggregates formed by dimyristoylphosphatidylcholine (DMPC) and dihexanoylphosphatidylcholine (DHPC) in aqueous solution at...
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[NMR paper] Influence of transmembrane peptides on bilayers of phosphatidylcholines with differen
Influence of transmembrane peptides on bilayers of phosphatidylcholines with different acyl chain lengths studied by solid-state NMR.
Related Articles Influence of transmembrane peptides on bilayers of phosphatidylcholines with different acyl chain lengths studied by solid-state NMR.
Biochim Biophys Acta. 2000 Dec 20;1509(1-2):335-45
Authors: Byström T, Strandberg E, Kovacs FA, Cross TA, Lindblom G
The molecular orientation in a lipid membrane of the peptide fragment VEYAGIALFFVAAVLTLWSMLQYLSAAR (phosphatidylglycerophosphate synthase (Pgs)...
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[NMR paper] Model of interaction between a cardiotoxin and dimyristoylphosphatidic acid bilayers
Model of interaction between a cardiotoxin and dimyristoylphosphatidic acid bilayers determined by solid-state 31P NMR spectroscopy.
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 Model of interaction between a cardiotoxin and dimyristoylphosphatidic acid bilayers determined by solid-state 31P NMR spectroscopy.
Biophys J. 1996 Apr;70(4):1737-44
Authors: Picard F,...
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[NMR paper] Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 2. E
Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 2. Evidence from phosphorus-31 NMR measurements.
Related Articles Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 2. Evidence from phosphorus-31 NMR measurements.
Biochemistry. 1991 Apr 23;30(16):3880-5
Authors: Spooner PJ, Watts A
31P NMR measurements were conducted to determine the structural and chemical environment of beef heart cardiolipin when bound to cytochrome c. 31P NMR line shapes infer that the majority of lipid remains...
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[NMR paper] Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. E
Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. Evidence from deuterium NMR measurements.
Related Articles Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. Evidence from deuterium NMR measurements.
Biochemistry. 1991 Apr 23;30(16):3871-9
Authors: Spooner PJ, Watts A
Deuterium NMR has been used to investigate the structure and dynamic state of cytochrome c complexed with bilayers of cardiolipin. Reductive methylation was employed to prepare lysyl cytochrome c, and deuterium...
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[NMR paper] One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11
One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla.
Related Articles One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla.
J Protein Chem. 1990 Apr;9(2):129-36
Authors: Dill K, Hu SH, Berman E, Pavia AA, Lacombe JM
One- and two-dimensional nuclear magnetic resonance (NMR) spectroscopy (at 11.7 Tesla) was used to gain some structural and spectral information about glycophorin AM, glycophorin AM tryptic glycopeptide, a related pentapeptide, and two related...