[Study of the denaturation of the N-terminal fragment of alpha-tropomyosin by NMR spectroscopy].
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.
Kutyshenko
V P
VP
Potekhin
S A
SA
Smalla
K Kh
KKh
D002152:Calorimetry, Differential Scanning; D006358:Hot Temperature; D009682:Magnetic Resonance Spectroscopy; D011489:Protein Denaturation; D014335:Tropomyosin / Q000737:chemistry*
D014335:Tropomyosin
Izuchenie denaturatsii N-kontsevogo fragmenta alpha-tropomiozina metodom IaMR-spektroskopii.