000081002 001__ 81002
000081002 005__ 20181221101932.0
000081002 037__ $$aBOOK_CHAP
000081002 245__ $$aOrientational fluctuations of melittin in lipid membranes as detected by time-resolved fluorescence anisotropy measurements
000081002 269__ $$a1987
000081002 260__ $$aBerlin$$bSpringer$$c1987
000081002 336__ $$aBook Chapters
000081002 490__ $$aSpringer Series in Biophysics$$v1
000081002 520__ $$aTime-resolved fluorescence anisotropy of the single tryptophan (Trp) residue of melittin was measured to assess the orientational fluctuations of the protein in lipid membranes above and below the lipid phase transition temp. (Tt). In phospholipid vesicles contg. melittin, 3 relaxation times were obsd. at temps. above Tt, whereas only 2 relaxation times were obsd. below Tt; the slowest of the 3 relaxations in fluid membranes was absent in the ordered membranes. In planar multibilayer membranes at temps. above Tt, 2 relaxation processes were detected, corresponding to the fastest and slowest relaxations in the fluid vesicles, whereas at temps. below Tt only 1 relaxation was obsd. The fastest relaxation was attributed to internal motion of the Trp ring, the intermediate relaxation was attributed to internal motions of the melittin helix coupled to motions of the nonhelical C-terminal segment, and the slowest relaxation was attributed to the rigid-body motions of the Trp-contg. helical segment of melittin. Order parameters were also evaluated. The method described for evaluating these data may be of general interest for characterizing protein fluctuations in lipid membranes. [on SciFinder (R)]
000081002 700__ $$0240645$$aVogel, Horst$$g106666
000081002 700__ $$aRigler, Rudolf
000081002 773__ $$q289-294$$tStructure, dynamics and function of biomolecules
000081002 909C0 $$0252153$$pLCPPM$$xU10170
000081002 909CO $$ooai:infoscience.tind.io:81002$$pSB$$pchapter
000081002 937__ $$aLCPPM-CHAPTER-1987-002
000081002 970__ $$a77/LCPPM
000081002 973__ $$aEPFL$$sPUBLISHED
000081002 980__ $$aCHAPTER