1
40
2
-
Text
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URL Address
<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>
Rights
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
Pages
1406-1416
Issue
3
Volume
80
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Dublin Core
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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
A point or period of time associated with an event in the lifecycle of the resource
2001
2001-03
Subject
The topic of the resource
Biophysics; cholesterol; conformational-changes; dynamics; lipid bilayers; micelles; nuclear magnetic-resonance; phospholipid-bilayers; protein-structure; solid-state nmr; x-ray-diffraction
Creator
An entity primarily responsible for making the resource
Prosser R S; Luchette P A; Westerman P W; Rozek A; Hancock R E W
Description
An account of the resource
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.
Identifier
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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
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.
URL Address
<a href="http://doi.org/10.1016/s0009-3084(97)00086-8" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/s0009-3084(97)00086-8</a>
Rights
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
Pages
109-115
Issue
1
Volume
90
Search for Full-text
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<p>Users with a NEOMED Library login can search for full-text journal articles at the following url: <a href="https://libraryguides.neomed.edu/home">https://libraryguides.neomed.edu/home</a></p>
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The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
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On the stability of the ripple phase in the DPPC/PLPC/water ternary system
Publisher
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Chemistry and Physics of Lipids
Date
A point or period of time associated with an event in the lifecycle of the resource
1997
1997-11
Subject
The topic of the resource
Biophysics; Biochemistry & Molecular Biology; gel; cholesterol; lysolecithin; membranes; nuclear-magnetic-resonance; water; transition; lipid bilayers; phospholipid-bilayers; Lipids; differential scanning calorimetry (DSC); lecithin; phosphatidylcholine; phosphatidylcholine bilayers; pretransition; scanning dilatometry (SD)
Creator
An entity primarily responsible for making the resource
Checchetti A; Chidichimo G; Golemme A; Grasso D; Imbardelli D; LaRosa C; Nicoletta F P; Westerman P W
Description
An account of the resource
The effect of incorporation of 1-palmitoyl-sn-glycero-3-phosphocholine (PLPC) on the structure of the P-beta' ripple mesophase in aqueous dispersions of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) has been studied by differential scanning calorimetry (DSC) and scanning dilatometry (SD). For samples containing 34 wt. % (H2O)-H-2 and 0-15 wt. % PLPC, a pretransition was observed by DSC. The pretransition disappears at 15 wt. % PLPC. The behavior of thermodynamic functions at the pretransition and main transition gives new insights on the structural changes produced by PLPC on bilayers of DPPC. (C) 1997 Elsevier Science Ireland Ltd.
Identifier
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<a href="http://doi.org/10.1016/s0009-3084(97)00086-8" target="_blank" rel="noreferrer noopener">10.1016/s0009-3084(97)00086-8</a>
Format
The file format, physical medium, or dimensions of the resource
Journal Article or Conference Abstract Publication
1997
Biochemistry & Molecular Biology
Biophysics
Checchetti A
Chemistry and Physics of Lipids
Chidichimo G
Cholesterol
differential scanning calorimetry (DSC)
Gel
Golemme A
Grasso D
Imbardelli D
Journal Article or Conference Abstract Publication
LaRosa C
LECITHIN
Lipid Bilayers
Lipids
lysolecithin
membranes
Nicoletta F P
nuclear-magnetic-resonance
phosphatidylcholine
phosphatidylcholine bilayers
phospholipid-bilayers
pretransition
scanning dilatometry (SD)
transition
Water
Westerman P W