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This paper is demonstrating the significance of strong, reciprocal protein 
lipid interactions in native thylakoids [DKP+99].
The techniques used here complement each other because 
electron paramagnetic resonance (EPR) detects only the spin 
label in these experiments and has a time window that is optimal 
for lipid chain dynamics, whereas Fourier transform infrared 
(FTIR) detects all lipid and protein vibrations simultaneously on 
a fast time scale [MM01]. FTIR spectroscopy is widely used to study 
protein secondary structure [JM95,AKM95] and lipid chain vibrations 
[MM01]. Motional coupling between large, relatively immobile 
membrane proteins and mobile fluid lipids results in motionally 
restricted protein-solvating [M99] first-shell lipids [M01,M01a,MH98]. This 
appears as 
immobile component in EPR spectra of spin-labeled lipid 
analogues as demonstrated in numerous membrane systems, 
including thylakoids. By quantitating these lipids, we have 
estimated changes in the size of protein assemblies of major 
thylakoid membrane protein complexes. The partitioning of 
2,2,6,6,-tetramethylpiperidine-1-oxyl (TEMPO) between membranous 
and aqueous environments depends on lipid packing 
and fluidity in the lipid bilayer and can be measured with EPR 
[Smirnov95]. A drop in the membranous TEMPO signal (in EPR) and 
a simultaneous increase in the CH2 vibration frequency (in 
FTIR) diagnosed a lipid transition that was interpreted as the 
formation of a nonbilayer phase. The temperature of this 
transition was found to vary during greening. The present study 
provides data on the time course of the thermal behavior of, and 
on the protein-lipid rearrangements in the thylakoid membrane 
during development.
