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