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・ Annuity (disambiguation)
・ Annuity (European)
・ Annuity function
・ Annular cutter
・ Annular dark-field imaging
・ Annular elastolytic giant-cell granuloma
・ Annular erythema of infancy
・ Annular fin
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・ Annular lake
・ Annular ligament (disambiguation)
・ Annular ligament of radius
・ Annular ligament of stapes
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Annular lipid shell
・ Annular pancreas
・ Annular pustular psoriasis
・ Annular tropical cyclone
・ Annular velocity
・ Annularia
・ Annularisca
・ Annularita
・ Annularodes
・ Annularops
・ Annulatascaceae
・ Annulatascus
・ Annulatin
・ Annulation
・ Annulene


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Annular lipid shell : ウィキペディア英語版
Annular lipid shell
''Annular lipids'' or ''shell lipids'' (also called ''boundary lipids'') represent a select set of lipids or lipidic molecules which preferentially 'bind' or stick to the surface of membrane proteins in biological cells. They constitute a layer, or an annulus/ shell, of lipids which are highly immobilized due to the existence of strong lipid-protein (binding) interactions. Polar headgroups of these lipids bind to the hydrophilic part of the membrane protein(s) at the inner and outer surfaces of lipid bilayer membrane. The hydrophobic surface of the membrane proteins is bound to the apposed lipid fatty acid chains of the membrane bilayer. For integral membrane proteins spanning the thickness of the membrane bilayer, these annular/shell lipids act like a lubricating layer on the proteins' surfaces, thereby facilitating almost free rotation and lateral diffusion of membrane proteins within the 2-dimensional expanse of the biological membrane(s). Outside the layer of shell/annular lipids, lipids are not tied down to protein molecules. However, they may be slightly restricted in their segmental motion freedom due to mild peer pressure of protein molecules, if present in high concentration, which arises from extended influence of protein-lipid interaction. Membrane areas away from protein molecules contain lamellar phase ''bulk lipids'', which are largely free from any restraining effects due to protein-lipid interactions. Thermal denaturation of membrane proteins may destroy the secondary and tertiary structure of membrane proteins, exposing newer surfaces to membrane lipids and therefore increasing the number of lipids molecules in the annulus/shell layer. This phenomenon can be studied by the spin label electron paramagnetic resonance technique.
==See more==

*Lipid
*Lipid bilayer
*Protein-lipid interaction
*Integral membrane protein
*Membrane lipids

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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