A H-2 NMR study of the interaction of a type II myosin with charged bilayers

A H-2 NMR study of the interaction of a type II myosin with charged bilayers

Bibliográfalaš dieđut
Váldodahkkit:	Areas, J, Glaubitz, C, Grobner, G, Watts, A
Materiálatiipa:	Journal article
Almmustuhtton:	2001

Geahča maid

Interaction of a type II myosin with biological membranes studied by 2H solid state NMR.
Dahkki: Arêas, J, et al.
Almmustuhtton: (1998)

Use of solid-state H-2 NMR for studying protein-lipid interactions at emulsion interfaces
Dahkki: Areas, J, et al.
Almmustuhtton: (1997)

Magic angle sample spinning NMR on uniformly aligned membranes: A new approach for biomembrane studies
Dahkki: Glaubitz, C, et al.
Almmustuhtton: (1998)

Spin label and 2H-NMR studies on the interaction of melanotropic peptides with lipid bilayers.
Dahkki: Biaggi, M, et al.
Almmustuhtton: (1996)

Probing membrane surfaces and the location of membrane-embedded peptides by (13)C MAS NMR using lanthanide ions.
Dahkki: Gröbner, G, et al.
Almmustuhtton: (1999)

Structural and orientational information of the membrane embedded M13 coat protein by (13)C-MAS NMR spectroscopy.
Dahkki: Glaubitz, C, et al.
Almmustuhtton: (2000)

M13 coat protein: Sub-nm high resolution structural studies of a membrane embedded peptide - A solid state NMR approach
Dahkki: Glaubitz, C, et al.
Almmustuhtton: (1997)

Phospholipid headgroup-headgroup electrostatic interactions in mixed bilayers of cardiolipin with phosphatidylcholines studied by 2H NMR.
Dahkki: Pinheiro, T, et al.
Almmustuhtton: (1994)

Interaction of the lantibiotic nisin with mixed lipid bilayers: a 31P and 2H NMR study.
Dahkki: Bonev, B, et al.
Almmustuhtton: (2000)

Molecular response of the lipid headgroup to bilayer hydration monitored by 2H-NMR.
Dahkki: Ulrich, A, et al.
Almmustuhtton: (1994)

Deuterium-MAS NMR spectroscopy on oriented membrane proteins: Applications to photointermediates of bacteriorhodopsin
Dahkki: Glaubitz, C, et al.
Almmustuhtton: (1999)

Solid-state NMR and simulation studies of equinatoxin II N-terminus interaction with lipid bilayers.
Dahkki: Lam, Y, et al.
Almmustuhtton: (2010)

Protein-lipid interactions is bacteriorhodopsin studied by solid state NMR
Dahkki: Mason, J, et al.
Almmustuhtton: (2000)

Membrane protein structure determination by solid state NMR.
Dahkki: Watts, A, et al.
Almmustuhtton: (1999)

Cytochrome c interactions with cardiolipin in bilayers: a multinuclear magic-angle spinning NMR study.
Dahkki: Spooner, P, et al.
Almmustuhtton: (1992)

Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 2. Evidence from phosphorus-31 NMR measurements.
Dahkki: Spooner, P, et al.
Almmustuhtton: (1991)

Photoreceptor rhodopsin: A structural and conformational study of 11-cis retinal in rhodopsin in oriented membranes by deuterium solid state NMR
Dahkki: Grobner, G, et al.
Almmustuhtton: (1997)

Lateral phase separation of anionic phospholipids in bilayers induced by peptides
Dahkki: Watts, A, et al.
Almmustuhtton: (1998)

Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phosphatidylglycerol bilayers, studied by 2H and 31P NMR spectroscopy.
Dahkki: Hayer-Hartl, M, et al.
Almmustuhtton: (1993)

Lipid specificity in the interaction of cytochrome c with anionic phospholipid bilayers revealed by solid-state 31P NMR.
Dahkki: Pinheiro, T, et al.
Almmustuhtton: (1994)

Effect of bacteriorhodopsin on the orientation of the headgroup of 1,2-dimyristoyl-sn-glycero-3-phosphocholine in bilayers: a 31P- and 2H-NMR study.
Dahkki: Gale, P, et al.
Almmustuhtton: (1992)

Structural descriptions of ligands in their binding site of integral membrane proteins at near physiological conditions using solid-state NMR
Dahkki: Watts, A, et al.
Almmustuhtton: (1998)

Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. Evidence from deuterium NMR measurements.
Dahkki: Spooner, P, et al.
Almmustuhtton: (1991)

Photoreceptor rhodopsin: structural and conformational study of its chromophore 11-cis retinal in oriented membranes by deuterium solid state NMR.
Dahkki: Gröbner, G, et al.
Almmustuhtton: (1998)

REDOR NMR on a hydrophobic peptide in oriented membranes.
Dahkki: Middleton, D, et al.
Almmustuhtton: (2000)

Structural studies on the transmembrane domain of phospholamban using H-1 and C-13 magic angle spinning NMR methods.
Dahkki: Ahmed, Z, et al.
Almmustuhtton: (1999)

Electrostatic peptide-lipid interactions of amyloid-beta peptide and pentalysine with membrane surfaces monitored by P-31 MAS NMR
Dahkki: Bonev, B, et al.
Almmustuhtton: (2001)

Solid state NMR studies of ligands bound to the nicotinic acetylcholine receptor.
Dahkki: Grobner, P, et al.
Almmustuhtton: (1998)

Solid state nuclear magnetic resonance (ss-NMR) of ligand protein interactions in the nicotinic acetylcholine receptor (nAChR)
Dahkki: Williamson, P, et al.
Almmustuhtton: (1996)

Stacking of charge-density waves in 2H-NbSe_{2} bilayers
Dahkki: F. Cossu, et al.
Almmustuhtton: (2024-11-01)

Structure determination of membrane-associated amyloid-beta-peptide by solid state NMR
Dahkki: Groebner, G, et al.
Almmustuhtton: (2000)

Solid state NMR studies of ligands bound to the nicotinic acetylcholine receptor.
Dahkki: Williamson, P, et al.
Almmustuhtton: (1998)

Headgroup interactions in mixed phospholipid bilayers.
Dahkki: Sixl, F, et al.
Almmustuhtton: (1983)

Probing membrane surfaces and location of membrane components by C-13 MAS NMR: Effect of paramagnetic shift reagents.
Dahkki: Glaubitz, C, et al.
Almmustuhtton: (1999)

Weak interaction of spectrin with phosphatidylcholine-phosphatidylserine multilayers: a 2H and 31P NMR study.
Dahkki: Bitbol, M, et al.
Almmustuhtton: (1989)

Combined quantitative and mechanistic study of drug-membrane interactions using a novel 2H NMR approach.
Dahkki: Middleton, D, et al.
Almmustuhtton: (2004)

Structural studies of prospholamban using solid-state magic-angle spinning (MAS) NMR methods.
Dahkki: Ahmed, Z, et al.
Almmustuhtton: (2000)

Quantifying the Charge Carrier Interaction in Metallic Twisted Bilayer Graphene Superlattices
Dahkki: Evgueni F. Talantsev
Almmustuhtton: (2021-05-01)

Identifying anisotropic constraints in multiply labeled bacteriorhodopsin by 15N MAOSS NMR: a general approach to structural studies of membrane proteins.
Dahkki: Mason, A, et al.
Almmustuhtton: (2004)

Multiple orientational constraints from bacteriorhodopsin in the purple membrane using 15N MAOSS solid-state NMR
Dahkki: Mason, A, et al.
Almmustuhtton: (2002)