Nuclear magnetic resonance methods to characterize lipid-protein interactions at membrane surfaces

Anthony Watts

doi:10.1007/bf00762300

Nuclear magnetic resonance methods to characterize lipid-protein interactions at membrane surfaces

Journal of Bioenergetics and Biomembranes ◽

10.1007/bf00762300 ◽

1987 ◽

Vol 19 (6) ◽

pp. 625-653 ◽

Cited By ~ 33

Author(s):

Anthony Watts

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Protein Interactions ◽

Membrane Surfaces ◽

Lipid Protein Interactions ◽

Nuclear Magnetic

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Phosphorus nuclear magnetic resonance studies of lipid-protein interactions: human erythrocyte glycophorin and phospholipids

Biochemistry ◽

10.1021/bi00431a036 ◽

1989 ◽

Vol 28 (5) ◽

pp. 2210-2215 ◽

Cited By ~ 23

Author(s):

P. L. Yeagle ◽

D. Kelsey

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Protein Interactions ◽

Human Erythrocyte ◽

Magnetic Resonance Studies ◽

Lipid Protein Interactions ◽

Nuclear Magnetic

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Nuclear magnetic resonance studies of lipid-protein interactions. A model of the dynamics and energetics of phosphatidylcholine bilayers that contain cytochrome c oxidase

Biochemistry ◽

10.1021/bi00645a015 ◽

1977 ◽

Vol 16 (26) ◽

pp. 5746-5755 ◽

Cited By ~ 45

Author(s):

Kenneth J. Longmuir ◽

Roderick A. Capaldi ◽

F. W. Dahlquist

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Cytochrome C ◽

Cytochrome C Oxidase ◽

Protein Interactions ◽

Magnetic Resonance Studies ◽

Lipid Protein Interactions ◽

Nuclear Magnetic

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13C Nuclear Magnetic Resonance Spectroscopic Evidence for Hydrophobic Lipid-Protein Interactions in Human High Density Lipoproteins

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.71.9.3696 ◽

1974 ◽

Vol 71 (9) ◽

pp. 3696-3700 ◽

Cited By ~ 79

Author(s):

W. Stoffel ◽

O. Zierenberg ◽

B. Tunggal ◽

E. Schreiber

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Protein Interactions ◽

High Density ◽

High Density Lipoproteins ◽

Spectroscopic Evidence ◽

13C Nuclear Magnetic Resonance ◽

Hydrophobic Lipid ◽

Lipid Protein Interactions ◽

Nuclear Magnetic

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- Nuclear Magnetic Resonance Studies of Carbohydrate–Protein Interactions

Structural Glycobiology ◽

10.1201/b12965-6 ◽

2012 ◽

pp. 44-61

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Protein Interactions ◽

Magnetic Resonance Studies ◽

Nuclear Magnetic

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Characterizing Carbohydrate-Protein Interactions by Nuclear Magnetic Resonance Spectroscopy

Biopolymers ◽

10.1002/bip.22329 ◽

2013 ◽

Vol 99 (10) ◽

pp. 796-806 ◽

Cited By ~ 13

Author(s):

Carole A. Bewley ◽

Syed Shahzad-ul-Hussan

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Magnetic Resonance Spectroscopy ◽

Nuclear Magnetic Resonance Spectroscopy ◽

Protein Interactions ◽

Resonance Spectroscopy ◽

Nuclear Magnetic

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Phospholipid-protein interactions in human low density lipoprotein detected by phosphorus-31 nuclear magnetic resonance

Biochemistry ◽

10.1021/bi00634a031 ◽

1977 ◽

Vol 16 (15) ◽

pp. 3487-3491 ◽

Cited By ~ 45

Author(s):

Philip L. Yeagle ◽

Robert G. Langdon ◽

R. Bruce Martin

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Protein Interactions ◽

Low Density Lipoprotein ◽

Density Lipoprotein ◽

Low Density ◽

Nuclear Magnetic

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Dynamical and temperature-dependent effects of lipid-protein interactions. Application of deuterium nuclear magnetic resonance and electron paramagnetic resonance spectroscopy to the same reconstitutions of cytochrome c oxidase

Biochemistry ◽

10.1021/bi00514a026 ◽

1981 ◽

Vol 20 (11) ◽

pp. 3152-3162 ◽

Cited By ~ 86

Author(s):

Michael R. Paddy ◽

F. W. Dahlquist ◽

James H. Davis ◽

Myer Bloom

Keyword(s):

Nuclear Magnetic Resonance ◽

Electron Paramagnetic Resonance ◽

Magnetic Resonance ◽

Protein Interactions ◽

Electron Paramagnetic Resonance Spectroscopy ◽

Resonance Spectroscopy ◽

Temperature Dependent ◽

Paramagnetic Resonance ◽

Lipid Protein Interactions ◽

Electron Paramagnetic

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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

Biochemistry ◽

10.1021/bi00365a015 ◽

1986 ◽

Vol 25 (17) ◽

pp. 4818-4825 ◽

Cited By ~ 15

Author(s):

Nicholas J. P. Ryba ◽

Christopher E. Dempsey ◽

Anthony Watts

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Nuclear Magnetic Resonance Study ◽

Magnetic Resonance Study ◽

Lipid Interactions ◽

Membrane Surfaces ◽

Bovine Rhodopsin ◽

Head Groups ◽

Nuclear Magnetic

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Exploring Weak, Transient Protein–Protein Interactions in Crowded In Vivo Environments by In-Cell Nuclear Magnetic Resonance Spectroscopy

Biochemistry ◽

10.1021/bi201287e ◽

2011 ◽

Vol 50 (43) ◽

pp. 9225-9236 ◽

Cited By ~ 115

Author(s):

Qinghua Wang ◽

Anastasia Zhuravleva ◽

Lila M. Gierasch

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Magnetic Resonance Spectroscopy ◽

Nuclear Magnetic Resonance Spectroscopy ◽

Protein Interactions ◽

Resonance Spectroscopy ◽

Protein Protein Interactions ◽

Nuclear Magnetic

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Oxygen-17 and sodium-23 nuclear magnetic resonance studies of myofibrillar protein interactions with water and electrolytes in relation to sorption isotherms

Journal of Agricultural and Food Chemistry ◽

10.1021/jf00081a009 ◽

1988 ◽

Vol 36 (3) ◽

pp. 437-444 ◽

Cited By ~ 12

Author(s):

Theodore S. Lioutas ◽

Ion C. Baianu ◽

Peter J. Bechtel ◽

Marvin P. Steinberg

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Protein Interactions ◽

Sorption Isotherms ◽

Myofibrillar Protein ◽

Magnetic Resonance Studies ◽

Nuclear Magnetic

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