Effect of denaturation on muscle proteins as studied by epr

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Abstract

The McConnell spin label technique with SH directed label was employed on surviving frog fiber bundles and on glycerinated rabbit psoas fibers in order to study the conformational changes in muscle proteins during urea and guanidine hydrochloride induced denaturation. The spin labeled muscle proteins showed a complex electron paramagnetic resonance (epr) spectrum, which was due to restricted motion of label. The correlation time was 1.43 nsec for weakly immobilized spin label and about 15 nsec for the strongly immobilized spin label in the case of surviving fiber bundles from frog. It has been concluded that the environment of spin label changes during denaturation evoked by urea and guanidine hydrochloride. The strongly immobilized signal disappears, and a significant increase can be observed in the average mobility of spin label. The conformational changes were found to be reversible at every urea concentration applied in the experiments.

Original languageEnglish
Pages (from-to)275-280
Number of pages6
JournalActa Biochimica et Biophysica Academiae Scientiarum Hungaricae
Volume8
Issue number4
Publication statusPublished - Dec 1 1973

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ASJC Scopus subject areas

  • Medicine(all)

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