Ca - LISM

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How efficient is hydrophobic matching?Trp fluorescence spectraW1.5Intensity1.00.5FreeTrp0.0300 320 340 360 380 400Wavelength (nm)
K + channel KcsA – How efficient is hydrophobic matching27 ÅC1816 ÅC1038 ÅC24
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 28 and 29: Reconstituted KcsAPhosphatidylcholi
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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