1
40
4
-
Text
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n/a
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Pages
49A-49A
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1
Volume
80
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Title
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Using O-2 to determine membrane immersion depth in bilayers by F-19 NMR a solid state and high-resolution NMR approach
Publisher
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Biophysical Journal
Date
A point or period of time associated with an event in the lifecycle of the resource
2001
2001-01
Subject
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Biophysics
Creator
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Prosser R S; Luchette P A; Westerman P W; Rozek A; Hancock R E W
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n/a
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Journal Article
2001
Biophysical Journal
Biophysics
Hancock R E W
Journal Article
Luchette P A
Prosser R S
Rozek A
Westerman P W
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
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n/a
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Pages
15A-15A
Issue
1
Volume
80
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Probing immersion depth & topology of membrane proteins by NMR. An ode to O-2
Publisher
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Biophysical Journal
Date
A point or period of time associated with an event in the lifecycle of the resource
2001
2001-01
Subject
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Biophysics
Creator
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Prosser R S; Luchette P A; Westerman P W; Rozek A; Hancock R E W
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n/a
Format
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Journal Article
2001
Biophysical Journal
Biophysics
Hancock R E W
Journal Article
Luchette P A
Prosser R S
Rozek A
Westerman P W
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
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<a href="http://doi.org/10.1016/s0006-3495(01)76113-9" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/s0006-3495(01)76113-9</a>
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Pages
1406-1416
Issue
3
Volume
80
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Title
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Determination of membrane immersion depth with O-2: A high-pressure F-19 NMR study
Publisher
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Biophysical Journal
Date
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2001
2001-03
Subject
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Biophysics; cholesterol; conformational-changes; dynamics; lipid bilayers; micelles; nuclear magnetic-resonance; phospholipid-bilayers; protein-structure; solid-state nmr; x-ray-diffraction
Creator
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Prosser R S; Luchette P A; Westerman P W; Rozek A; Hancock R E W
Description
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Oxygen is known to partition with an increasing concentration gradient toward the hydrophobic membrane interior. At partial pressures (P-O2) of 100 Atm or more, this concentration gradient is sufficient to induce paramagnetic effects that depend sensitively on membrane immersion depth. This effect is demonstrated for the fluorine nucleus by depth-dependent: paramagnetic shifts and spin-lattice relaxation rates, using a fluorinated detergent, CF3(CF2)(5)C2H4-O-maltose (TFOM), reconstituted into a lipid bilayer model membrane system, To interpret the spin-lattice relaxation rates (R-1(P)) in terms of a precise immersion depth, two specifically fluorinated cholesterol species (6-fluorocholesterol and 25-fluorocholesterol), whose membrane immersion depths were independently estimated, were studied by F-19 NMR. The paramagnetic relaxation rates, R-1(P), of the cholesterol species were then used to parameterize a Gaussian profile that directly relates R-1(P) to immersion depth z.: This same Gaussian curve could then be used to determine the membrane immersion depth of all six fluorinated chain positions of TFOM and of two adjacent residues of specifically fluorinated analogs of the antibacterial peptide indolicidin. The potential of this method for determination of immersion depth and topology of membrane proteins is discussed.
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<a href="http://doi.org/10.1016/s0006-3495(01)76113-9" target="_blank" rel="noreferrer noopener">10.1016/s0006-3495(01)76113-9</a>
Format
The file format, physical medium, or dimensions of the resource
Journal Article
2001
Biophysical Journal
Biophysics
Cholesterol
conformational-changes
dynamics
Hancock R E W
Journal Article
Lipid Bilayers
Luchette P A
micelles
nuclear magnetic-resonance
phospholipid-bilayers
Prosser R S
protein-structure
Rozek A
solid-state nmr
Westerman P W
x-ray-diffraction
-
Text
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<a href="http://doi.org/10.1073/pnas.170295297" target="_blank" rel="noreferrer noopener">http://doi.org/10.1073/pnas.170295297</a>
Pages
9967–9971
Issue
18
Volume
97
Dublin Core
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Title
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Using O2 to probe membrane immersion depth by 19F NMR.
Publisher
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Proceedings of the National Academy of Sciences of the United States of America
Date
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2000
2000-08
Subject
The topic of the resource
*Hydrocarbons; *Oxygen; Biological; Cyclic N-Oxides; Dimyristoylphosphatidylcholine/*chemistry; Fluorinated; Fluorine; Lipid Bilayers/*chemistry; Magnetic Resonance Spectroscopy/*methods; Maltose/*analogs & derivatives; Models; Phospholipid Ethers/*chemistry; Pressure; Spin Labels
Creator
An entity primarily responsible for making the resource
Prosser R S; Luchette P A; Westerman P W
Description
An account of the resource
A fluorinated detergent, CF(3)(CF(2))(5)C(2)H(4)-O-maltose, was reconstituted into a lipid bilayer model membrane system to demonstrate the feasibility of determining solvent accessibility and membrane immersion depth of each fluorinated group by (19)F NMR. Apolar oxygen, which is known to partition with an increasing concentration gradient toward the hydrophobic membrane interior, exhibits a range of paramagnetic relaxation effects on (19)F nuclei, depending on its depth in the membrane. This effect, which is predominately associated with spin-lattice relaxation rates (R(1)) and chemical shifts, can be amplified greatly with minimal line broadening by increasing the partial pressure of O(2) at least 100-fold (i.e., P(O(2)) greater than 20 bar). The differences of longitudinal relaxation rates at 20 bar of oxygen pressure to those under ambient pressure (R(1)(20bar) - R(1)(0)) are largest for those fluorine groups expected to be most deeply buried in the membrane bilayer. This result contrasts with the reverse trend, which is observed on addition of a membrane surface-associated paramagnetic species, 4-(N,N-dimethyl-N-hexadecyl) ammonium-2,2,6,6-tetramethylpiperidine-1-oxyl iodide (CAT-16) at ambient pressures. Thus, differential relaxation rates may be observed in (19)F-labeled membrane-associated molecules resulting from the addition of apolar oxygen under high pressure. The results demonstrate that the degree of solvent accessibility and membrane immersion depth of specific fluorinated species in membrane-associated macromolecules can be probed by (19)F NMR.
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<a href="http://doi.org/10.1073/pnas.170295297" target="_blank" rel="noreferrer noopener">10.1073/pnas.170295297</a>
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Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
*Hydrocarbons
*Oxygen
2000
Biological
Cyclic N-Oxides
Dimyristoylphosphatidylcholine/*chemistry
Fluorinated
Fluorine
Lipid Bilayers/*chemistry
Luchette P A
Magnetic Resonance Spectroscopy/*methods
Maltose/*analogs & derivatives
Models
Phospholipid Ethers/*chemistry
Pressure
Proceedings of the National Academy of Sciences of the United States of America
Prosser R S
Spin Labels
Westerman P W