Ca - LISM

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Reconstituted KcsAPhosphatidylcholineChain Length1.4 C101.21.00.80.60.40.20.0FreeTrpC18C24-0.2300 320 340 360 380 400Wavelength (nm)
Tryptophan residues do not change their environmentwith changing bilayer thicknessC18C10C24Hydrophobic matching is highly efficientEither lipid distorts to match proteinor protein distorts to match lipidor both
Page 1: Saulieu October 2004Protein-Lipid I
Page 4 and 5: Lipid as solventBacteriorhodopsinLi
Page 6 and 7: The importance of Annular LipidThe
Page 8 and 9: Effect of Lipid headgroupCalcium AT
Page 14 and 15: Calcium accumulation (nmoles/mg pro
Page 16 and 17: Ca outSlippage and LeakSlippageATPh
Page 18 and 19: SarcoplasmicReticulumNerveDepolaris
Page 20 and 21: Sarcoplasmic reticulum contains sar
Page 26 and 27: How efficient is hydrophobic matchi
Page 30 and 31: Hydrophobic MismatchBilayer Distort
Page 32 and 33: Fluorescence quenchingin mixtures o
Page 34 and 35: Relative binding constant2.01.51.00
Page 36 and 37: RCalcium ATPaseChangingBilayer thic
Page 38 and 39: Diacylglycerol kinase of E. coliPer
Page 40 and 41: Hydrophobic mismatchCalcium ATPaseC
Page 42 and 43: Fluorescence quenchingTrp containin
Page 44 and 45: Hydrophobic matching between the bi
Page 46 and 47: Trp at ends of helices are not cons
Page 48 and 49: Use of Trp fluorescence to define h
Page 50 and 51: D6825 A O L69V91L92R11Y94D16
Page 52 and 53: KcsAnon-annularlipidanionicannularl
Page 54 and 55: KcsA Trp quenchingnon-annularoF/F1.
Page 56 and 57: Lipid-Protein InteractionsAnnular l

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