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eralordersofmagnitude.Thus,theseresultsnotonlycomplementedthe
structuraldataobtainedbydiffractionmethodsandNMR,butallowedob-
taininganewimportantinformationthatcannotbederivedfromtheresults
ofstructuralstudies.Proteinmoleculesinsolutionshavestartedtobecon-
sideredasmicroscopicbodies(micro-phases),thecomposition,molecular
order,dynamicsandthermodynamicsofwhicharequitedifferentfromthat
ofsurroundingmacro-phase,thesolvent.
Theattractivefeaturesofthisapproachwererapidlyrecognized,and
otherapplicationsfollowed,mainlyinthefieldsofpolymerscience,micellar
colloidchemistryandmembranebiology.Themethodology,whichemerged
withthediscoveryoftheRed-Edgeeffects,stimulatedthedevelopmentof
researchinavarietyofnewareas.Itwasfoundthatdifferentexcited-statere-
actionsintheconditionsofslowmobilityintheenvironmentoftheexcited
speciesexhibitstrongsite-selectivity.Amongtheseintramolecularreactions
areexcited-stateisomerizationsandalsoelectron,protonandexcitationen-
ergytransfers(Demchenko&Sytnik1991b,Nemkovichetal.1981).These
low-barrierreactionsmaybeconsideredasanalogsofcatalyticand
biocatalyticground-statereactions,andthisopensthepossibilitiestostudy
theirdependenceondynamicsofproteinmatrixonafastscaleofnuclear
motions(Demchenko1994).
Thus,theobservationsoftheRed-Edgeeffectsfeaturesimplicityinperfor-
mance,flexibility,possibilityofstudiesinthebroadrangeoftemperaturesin
theconditionsofmolecularrelaxationsandofcouplingwithavarietyof
physicalandchemicaltransformations(Demchenko2002).Thisisthereason
whytheyachievedsogreatpopularity.
