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Study of the denaturation of the N-terminal fragment of alpha-tropomyosin by NMR spectroscopy

Kutyshenko, V.P.; Potekhin, S.A.; Smalla, K.K.

Biofizika 36(5): 762-769

1991

ISSN/ISBN: 0006-3029
PMID: 1799590
Document Number: 381119
Heat denaturation of the CN1A fragment (11-127) of alpha-tropomyosin was studied by NMR spectroscopy. It was shown that increasing temperature makes the fragment go through some discrete states distinguished by the spectrum of tyrosine-60. Three of these states are characterized by differences in the compact surrounding of the single tyrosine. There is a definite correlation between the observed microstates of tyrosine-60 and the realized microstates of the fragment. The appearance of different states of tyrosine is suggested to be caused by a change in the structure of its environment due to denaturation of other, rather remote regions, i.e. by appreciable mutual effects of different regions of the alpha-superhelix.

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