1999
DOI: 10.1016/s0006-3495(99)77257-7
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Experimental Evidence for Hydrophobic Matching and Membrane-Mediated Interactions in Lipid Bilayers Containing Gramicidin

Abstract: Hydrophobic matching, in which transmembrane proteins cause the surrounding lipid bilayer to adjust its hydrocarbon thickness to match the length of the hydrophobic surface of the protein, is a commonly accepted idea in membrane biophysics. To test this idea, gramicidin (gD) was embedded in 1, 2-dilauroyl-sn-glycero-3-phosphocholine (DLPC) and 1, 2-myristoyl-sn-glycero-3-phosphocholine (DMPC) bilayers at the peptide/lipid molar ratio of 1:10. Circular dichroism (CD) was measured to ensure that the gramicidin w… Show more

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Cited by 254 publications
(238 citation statements)
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“…The insertion and orientation of polypeptides, as well as the activity of integral membrane proteins critically depends on bilayer thickness (Lee 2004). On the other hand, because of the structural flexibility of lipid hydrocarbon chains, a membrane can adjust its thickness in order to minimize unfavourable thermodynamic interactions between water and hydrophobic protein surfaces, a process known as hydrophobic matching (Harroun et al 1999). An example of this is sarcoplasmic reticulum Ca 2+ -transporting ATPase reconstituted into bilayers made up of monounsaturated phospholipids and a biological detergent (Karlovská et al 2006).…”
Section: Introductionmentioning
confidence: 99%
“…The insertion and orientation of polypeptides, as well as the activity of integral membrane proteins critically depends on bilayer thickness (Lee 2004). On the other hand, because of the structural flexibility of lipid hydrocarbon chains, a membrane can adjust its thickness in order to minimize unfavourable thermodynamic interactions between water and hydrophobic protein surfaces, a process known as hydrophobic matching (Harroun et al 1999). An example of this is sarcoplasmic reticulum Ca 2+ -transporting ATPase reconstituted into bilayers made up of monounsaturated phospholipids and a biological detergent (Karlovská et al 2006).…”
Section: Introductionmentioning
confidence: 99%
“…This occurs when TM proteins of varying lengths cause localized thickening and thinning of the membrane bilayer. Proteins are approximately 400 times less compressible than the phospholipids in a membrane bilayer, 38 which is a consequence of the increased capacity of phospholipids to undergo stretching and compression. While it is the phospholipids that usually undergo the structural remodeling to produce hydrophobic matching, the TM proteins can also adjust their thickness by lateral association and tilting of TM segments.…”
Section: Forces and Neutral Hydrogen Bonding)mentioning
confidence: 99%
“…As a result, the elastic decay length of protein-induced lipid bilayer thickness deformations [24][25][26] is comparable to the typical edge-to-edge spacing of proteins in cell membranes [7], yielding thickness-mediated interactions between membrane proteins [7,[27][28][29][30]. For the small protein separations relevant for cell membranes, thickness-mediated interactions between integral membrane proteins can be > 10 k B T in magnitude [7,31] and, depending on the hydrophobic thickness of neighboring membrane proteins, be energetically favorable or unfavorable.…”
Section: Introductionmentioning
confidence: 99%
“…We focus here on protein-induced lipid bilayer thickness deformations, which have been found [2][3][4][5][6][7][8][9][27][28][29][30] to play central roles in regulation of protein function and bilayer-mediated protein interactions in a wide range of experimental systems [10, 11, 24-28, 31, 38-47, 81-83, 88-97]. Using this mathematical framework we have shown previously that the shape of integral membrane proteins, and resulting structure of lipid bilayer thickness deformations, can play a crucial role in the regulation of protein function by lipid bilayers [47,88], and that bilayer thicknessmediated interactions between integral membrane proteins can be strongly directional and dependent on protein shape [46,47,89,97].…”
Section: Introductionmentioning
confidence: 99%