Nuclear magnetic resonance methods to characterize lipid-protein interactions at membrane surfaces. by Watts, A

“…Classical methods for obtaining structural information about biomolecules, including X-ray diffraction, electron microscopy, and more recently high-resolution 2D nuclear magnetic resonance techniques are inappropriate for all but the simplest of membrane problems. …”

Dynamic structure and phase behavior of dimyristoylphosphatidylethanolamine bilayers studied by deuterium nuclear magnetic resonance. by Marsh, D, Watts, A, Smith, I

“…The dynamic structure of dimyristoylphosphatidylethanolamine bilayers has been studied by deuterium nuclear magnetic resonance spectroscopy of the perdeuterated sn-2 chain. …”

Deuterium and phosphorus nuclear magnetic resonance studies on the binding of polymyxin B to lipid bilayer-water interfaces. by Sixl, F, Watts, A

Probing the structure of a potent acetylcholinesterase inhibitor in the binding site using solid state nuclear magnetic resonance. by Goodall, S, Spooner, P, Middleton, D, Howe, P, Watts, A

Dynamics in a protein-lipid complex: nuclear magnetic resonance measurements on the headgroup of cardiolipin when bound to cytochrome c. by Spooner, P, Duralski, A, Rankin, SE, Pinheiro, T, Watts, A

“…Deuterium and phosphorus nuclear magnetic resonance (NMR) has been used to investigate the dynamics of slow motional processes induced in bilayer cardiolipin upon binding with cytochrome c. 31P NMR line shapes suggest that protein binding induces less restricted, isotropic-like motions in the lipid phosphates within the ms time scale of this measurement. …”

Structural information on a membrane transport protein from nuclear magnetic resonance spectroscopy using sequence-selective nitroxide labeling. by Spooner, P, Veenhoff, L, Watts, A, Poolman, B

“…Cross-polarization magic-angle spinning nuclear magnetic resonance spectroscopy (NMR) could selectively distinguish binding of (13)C-labeled substrate to just 50-60 nmol of LacS(K373C) in the native fluid membranes. …”

Evidence from deuterium nuclear magnetic resonance for the temperature-dependent reversible self-association of erythrocyte band 3 in dimyristoylphosphatidylcholine bilayers. by Dempsey, C, Ryba, N, Watts, A

“…Electron micrographs of negatively stained complexes showed that this method produced large vesicles of greater than 300-nm diameter. Deuterium nuclear magnetic resonance (NMR) spectra from the choline methyl deuterons in bilayer lipid above the liquid-crystal-gel phase transition temperature were shown to change systematically with increasing concentrations of band 3 in the bilayers. …”

Solid state nuclear magnetic resonance (ss-NMR) of ligand protein interactions in the nicotinic acetylcholine receptor (nAChR) by Williamson, P, Grobner, G, Miller, K, Watts, A

A deuterium and phosphorus-31 nuclear magnetic resonance study of the interaction of melittin with dimyristoylphosphatidylcholine bilayers and the effects of contaminating phospholipase A2. by Dempsey, C, Watts, A

“…The interaction of bee venom melittin with dimyristolphosphatidylcholine (DMPC) selectively deuteriated in the choline head group has been studied by deuterium and phosphorus-31 nuclear magnetic resonance (NMR) spectroscopy. The action of residual phospholipase A2 in melittin samples resulted in mixtures of DMPC and its hydrolytic products that underwent reversible transitions at temperatures between 30 and 35 degrees C from extended bilayers to micellar particles which gave narrow single-line deuterium and phosphorus-31 NMR spectra. …”

Interactions between phospholipid head groups at membrane interfaces: a deuterium and phosphorus nuclear magnetic resonance and spin-label electron spin resonance study. by Sixl, F, Watts, A

“…The head group interactions in fully hydrated, mixed bilayers of 1,2-dimyristoyl-sn-glycero-3-phosphocholine and 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol, specifically deuterated in the head groups at the α- and β-methylene and N(CD3)3 positions, have been investigated by deuterium and phosphorus-31 nuclear magnetic resonance (NMR) and 2,2,6,6-tetramethylpiperidinyl-1-oxy (Tempo) spin-label electron spin resonance (ESR) studies at pH 7.5. …”

Protein-lipid interactions at membrane surfaces: a deuterium and phosphorus nuclear magnetic resonance study of the interaction between bovine rhodopsin and the bilayer head groups of dimyristoylphosphatidylcholine. by Ryba, N, Dempsey, C, Watts, A

“…Complexes produced with rhodopsin from frozen retina produced an absorption maximum at 478 nm after photobleaching whereas rhodopsin from fresh retina could be bleached more completely to an absorption maximum at 380 nm. Deuterium nuclear magnetic resonance (NMR) spectra from the lipid head groups of bilayers above the gel to liquid-crystalline phase transition temperature were shown to be sensitive in a systematic way to the presence of rhodopsin which could be bleached to 380 nm. …”

Bacteriorhodopsin/phospholipid interactions - a study by ³¹P- and ²H-NMR by Gale, P, Gale, Paul

Subjects: “…Nuclear magnetic resonance…”

SELECTIVE PROTEIN LIPID INTERACTIONS AT MEMBRANE SURFACES - A DEUTERIUM AND PHOSPHORUS NUCLEAR MAGNETIC-RESONANCE STUDY OF THE ASSOCIATION OF MYELIN BASIC-PROTEIN WITH THE BILAYER HEAD GROUPS OF DIMYRISTOYLPHOSPHATIDYLCHOLINE AND DIMYRISTOYLPHOSPHATIDYLGLYCEROL by Sixl, F, Brophy, P, Watts, A

“…The lipids were selectively deuterated at all positions in their polar head groups, the motional rate and amplitude of which were characterized by deuterium and phosphorus-31 nuclear magnetic resonance (NMR). Basic protein, which binds peripherally to membranes, did not perturb any part of the head groups in phosphatidylcholine bilayers in such a way as to induce any significant changes in the NMR spectra. …”

Direct determination by 2H-NMR of the ionization state of phospholipids and of a local anaesthetic at the membrane surface. by Watts, A, Poile, T

“…Here we show how studies by deuterium nuclear magnetic resonance of non-perturbing deuterons, specifically placed at the membrane polar-apolar interface, can give direct information about the electrostatics at a membrane surface.…”

Direct determination by 2H-NMR of the ionization state of phospholipids and of a local anaesthetic at the membrane surface by Watts, A, Poile, T

“…Here we show how studies by deuterium nuclear magnetic resonance of non-perturbing deuterons, specifically placed at the membrane polar-apolar interface, can give direct information about the electrostatics at a membrane surface. © 1986.…”

Phospholipid phase transitions as revealed by NMR. by Watts, A, Spooner, P

“…Within the bilayer form, laterally separated phases may be induced as a result of surface electrostatic associations, thermotropic behaviour, lipid-protein interactions or because of molecular mismatch between chemically distinct phospholipids. Nuclear magnetic resonance (NMR) methods, designed to exploit the properties of either indigenous nuclei or isotopic labels introduced specifically into a phospholipid, can be used in some cases to describe the molecular properties and behaviour of phospholipids in both macroscopically distinct phases and in molecularly distinct phases within the same polymorphic state. …”

31P-CP-MAS NMR studies on TPP+ bound to the ion-coupled multidrug transport protein EmrE. by Glaubitz, C, Gröger, A, Gottschalk, K, Spooner, P, Watts, A, Schuldiner, S, Kessler, H

“…The binding of tetraphenylphosphonium (TPP+) to EmrE, a membrane-bound, 110 residue Escherichia coli multidrug transport protein, has been observed by 31P cross-polarisation-magic-angle spinning nuclear magnetic resonance spectroscopy (CP-MAS NMR). EmrE has been reconstituted into dimyristoyl phosphatidylcholine bilayers. …”

THE DEPENDENCE OF PHOSPHOLIPID HEADGROUP MOBILITY ON HYDRATION AS STUDIED BY DEUTERIUM-NMR SPIN-LATTICE RELAXATION-TIME MEASUREMENTS by Ulrich, A, Volke, F, Watts, A

“…The dependence of the head-group mobility of DOPC-d9 (dioleylphosphatidylcholine, deuterated at its choline methyl groups) on hydration has been studied in multibilayer dispersions by deuterium nuclear magnetic resonance (2H-NMR) spin-lattice (T1) relaxation time measurements. …”

Structural and orientational information of the membrane embedded M13 coat protein by (13)C-MAS NMR spectroscopy. by Glaubitz, C, Gröbner, G, Watts, A

“…Oriented and unoriented M13 coat protein, incorporated into dimyristoyl phosphatidylcholine bilayers, has been studied by (13)C-magic angle spinning nuclear magnetic resonance (MAS NMR) spectroscopy. Rotational resonance experiments provided two distance constraints between Calpha and Candz.dbnd6;O positions of the labelled residues Val-29/Val-30 (0.4+/-0.5nm) and Val-29/Val-31 (0.45+/-0. 5nm) in its hydrophobic domain. …”

Combined quantitative and mechanistic study of drug-membrane interactions using a novel 2H NMR approach. by Middleton, D, Reid, D, Watts, A

“…A new (2)H nuclear magnetic resonance (NMR) approach has been developed here that quantifies the affinity of (2)H-labeled small molecules for different phospholipid membranes and, simultaneously, provides information on the mechanism of the drug-membrane interaction. …”