Mechanically, magnetically, and "rotationally aligned" membrane proteins in phospholipid bilayers give equivalent angular constraints for NMR structure determination.
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Structure determination of membrane proteins by nuclear magnetic resonance spectroscopyNMR structures of membrane proteins in phospholipid bilayersStructure of the chemokine receptor CXCR1 in phospholipid bilayersStructure Determination of a Membrane Protein in ProteoliposomesThe Structure of the Mercury Transporter MerF in Phospholipid Bilayers: A Large Conformational Rearrangement Results from N-Terminal TruncationMembrane protein structure from rotational diffusionThe development of solid-state NMR of membrane proteins.Observing the overall rocking motion of a protein in a crystalStructure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR.Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.A general assignment method for oriented sample (OS) solid-state NMR of proteins based on the correlation of resonances through heteronuclear dipolar couplings in samples aligned parallel and perpendicular to the magnetic fieldSolid-state NMR and membrane proteins.Local and global dynamics of the G protein-coupled receptor CXCR1.Improved 1H amide resonance line narrowing in oriented sample solid-state NMR of membrane proteins in phospholipid bilayers.Experiments optimized for magic angle spinning and oriented sample solid-state NMR of proteins.Resonance assignments of a membrane protein in phospholipid bilayers by combining multiple strategies of oriented sample solid-state NMR.Structure determination of membrane proteins in five easy piecesApplications of NMR to membrane proteins.Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of rotationally aligned membrane proteins in phospholipid bilayers.Correlating lipid bilayer fluidity with sensitivity and resolution of polytopic membrane protein spectra by solid-state NMR spectroscopy.Modulation of cross polarization in motionally averaged solids by Variable Angle Spinning NMRStructure determination of membrane proteins in their native phospholipid bilayer environment by rotationally aligned solid-state NMR spectroscopy.Solid-state NMR structures of integral membrane proteins.New applications of solid-state NMR in structural biology
P2860
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P2860
Mechanically, magnetically, and "rotationally aligned" membrane proteins in phospholipid bilayers give equivalent angular constraints for NMR structure determination.
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2010 nî lūn-bûn
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2010年の論文
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2010年学术文章
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2010年学术文章
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2010年学术文章
@zh-hans
2010年学术文章
@zh-my
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@zh-sg
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name
Mechanically, magnetically, an ...... r NMR structure determination.
@en
Mechanically, magnetically, an ...... r NMR structure determination.
@nl
type
label
Mechanically, magnetically, an ...... r NMR structure determination.
@en
Mechanically, magnetically, an ...... r NMR structure determination.
@nl
prefLabel
Mechanically, magnetically, an ...... r NMR structure determination.
@en
Mechanically, magnetically, an ...... r NMR structure determination.
@nl
P2093
P2860
P356
P1476
Mechanically, magnetically, an ...... or NMR structure determination
@en
P2093
Anna A De Angelis
Bibhuti B Das
Sang Ho Park
Stanley J Opella
P2860
P304
13995-14003
P356
10.1021/JP106043W
P407
P50
P577
2010-11-01T00:00:00Z