Related ArticlesSolubilization and localization of weakly polar lipids in unsonicated egg phosphatidylcholine: A 13C MAS NMR study.
Biochemistry. 1991 Mar 19;30(11):2894-902
Authors: Hamilton JA, Fujito DT, Hammer CF
The weakly polar lipids cholesteryl ester, triacylglycerol, and diacylglycerol incorporate to a limited extent into the lamellar structure of small unilamellar vesicles. The localization of the carbonyl group(s) at the aqueous interface was detected by [13C]carbonyl chemical shift changes relative to the neat unhydrated lipid [Hamilton, J.A., & Small, D.M. (1981) Proc. Natl. Acad. Sci. U.S.A. 78, 6878-6882; Hamilton, J.A., & Small, D.M. (1982) J. Biol. Chem. 257, 7318-7321; Hamilton, J.A., Bhamidipati, S.B., Kodali, D.R., & Small, D.M. (1991) J. Biol. Chem. 266, 1177-1186]. This study uses 13C NMR to investigate the interactions of these lipids with unsonicated (multilamellar) phosphatidylcholine, a model system for cellular membranes and surfaces of emulsion particles with low curvature. Magic angle spinning reduced the broad lines of the unsonicated dispersions to narrow lines comparable to those from sonicated dispersions. [13C]Carbonyl chemical shifts revealed incorporation of the three lipids into the lamellar structure of the unsonicated phospholipids and a partial hydration of the carbonyl groups similar to that observed in small vesicles. Other properties of interfacial weakly polar lipids in multilayers were similar to those in small unilamellar bilayers. There is thus a general tendency of weakly polar lipids to incorporate at least to a small extent into the lamellar structure of phospholipids and take on interfacial properties that are distinct from their bulk-phase properties. This pool of surface-located lipid is likely to be directly involved in enzymatic transformations and protein-mediated transport. The 13C magic angle spinning NMR method may be generally useful for determining the orientation of molecules in model membranes.
[NMR paper] Paramagnetic NMR study of Cu(2+)-IDA complex localization on a protein surface and it
Paramagnetic NMR study of Cu(2+)-IDA complex localization on a protein surface and its application to elucidate long distance information.
Related Articles Paramagnetic NMR study of Cu(2+)-IDA complex localization on a protein surface and its application to elucidate long distance information.
FEBS Lett. 2004 May 21;566(1-3):157-61
Authors: Nomura M, Kobayashi T, Kohno T, Fujiwara K, Tenno T, Shirakawa M, Ishizaki I, Yamamoto K, Matsuyama T, Mishima M, Kojima C
The paramagnetic metal chelate complex Cu(2+)-iminodiacetic acid (Cu(2+)-IDA) was...
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[NMR paper] Spatial localization of ligand binding sites from electron current density surfaces c
Spatial localization of ligand binding sites from electron current density surfaces calculated from NMR chemical shift perturbations.
Related Articles Spatial localization of ligand binding sites from electron current density surfaces calculated from NMR chemical shift perturbations.
J Am Chem Soc. 2002 Oct 2;124(39):11758-63
Authors: McCoy MA, Wyss DF
Rapid, accurate structure determination of protein-ligand complexes is an essential component in structure-based drug design. We have developed a method that uses NMR protein chemical shift...
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[NMR paper] Membrane protein topology probed by (1)H spin diffusion from lipids using solid-state
Membrane protein topology probed by (1)H spin diffusion from lipids using solid-state NMR spectroscopy.
Related Articles Membrane protein topology probed by (1)H spin diffusion from lipids using solid-state NMR spectroscopy.
J Am Chem Soc. 2002 Feb 6;124(5):874-83
Authors: Huster D, Yao X, Hong M
We describe a two-dimensional solid-state NMR technique to investigate membrane protein topology under magic-angle spinning conditions. The experiment detects the rate of (1)H spin diffusion from the mobile lipids to the rigid protein. While spin...
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[NMR paper] Resolution of individual lipids in mixed phospholipid membranes and specific lipid-cy
Resolution of individual lipids in mixed phospholipid membranes and specific lipid-cytochrome c interactions by magic-angle spinning solid-state phosphorus-31 NMR.
Related Articles Resolution of individual lipids in mixed phospholipid membranes and specific lipid-cytochrome c interactions by magic-angle spinning solid-state phosphorus-31 NMR.
Biochemistry. 1994 Mar 8;33(9):2459-67
Authors: Pinheiro TJ, Watts A
A model of the inner mitochondrial membrane was constructed with dioleoyphosphatidylcholine (PC), dioleoylphosphatidylethanolamine...
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[NMR paper] Resolution of individual lipids in mixed phospholipid membranes and specific lipid-cy
Resolution of individual lipids in mixed phospholipid membranes and specific lipid-cytochrome c interactions by magic-angle spinning solid-state phosphorus-31 NMR.
Related Articles Resolution of individual lipids in mixed phospholipid membranes and specific lipid-cytochrome c interactions by magic-angle spinning solid-state phosphorus-31 NMR.
Biochemistry. 1994 Mar 8;33(9):2459-67
Authors: Pinheiro TJ, Watts A
A model of the inner mitochondrial membrane was constructed with dioleoyphosphatidylcholine (PC), dioleoylphosphatidylethanolamine...
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[NMR paper] Detergent delipidation and solubilization strategies for high-resolution NMR of the m
Detergent delipidation and solubilization strategies for high-resolution NMR of the membrane protein bacteriorhodopsin.
Related Articles Detergent delipidation and solubilization strategies for high-resolution NMR of the membrane protein bacteriorhodopsin.
J Biol Chem. 1991 Jun 5;266(16):10066-9
Authors: Seigneuret M, Neumann JM, Rigaud JL
High-resolution NMR studies of bacteriorhodopsin require the availability of the detergent-solubilized protein with both high concentration and small rotational correlation time. A procedure is described for...
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[NMR paper] Identification and localization of bound internal water in the solution structure of
Identification and localization of bound internal water in the solution structure of interleukin 1 beta by heteronuclear three-dimensional 1H rotating-frame Overhauser 15N-1H multiple quantum coherence NMR spectroscopy.
Related Articles Identification and localization of bound internal water in the solution structure of interleukin 1 beta by heteronuclear three-dimensional 1H rotating-frame Overhauser 15N-1H multiple quantum coherence NMR spectroscopy.
Biochemistry. 1990 Jun 19;29(24):5671-6
Authors: Clore GM, Bax A, Wingfield PT, Gronenborn AM
...
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Precise structural determination of weakly binding peptides by utilizing dihedral ang
Abstract Structural determination of target-bound conformations of peptides is of primary importance for the optimization of peptide ligands and peptideā??mimetic design. In the structural determination of weakly binding ligands, transferred nuclear Overhauser effect (TrNOE) methods have been widely used. However, not many distance constraints can be obtained from small peptide ligands by TrNOE, especially for peptides bound to a target molecule in an extended conformation. Therefore, for precise structural determination of weakly binding peptides, additional structural constraints are...