Thermal unfolding of various human non-muscle isoforms of tropomyosinстатья

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Дата последнего поиска статьи во внешних источниках: 3 июня 2020 г.

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[1] Thermal unfolding of various human non-muscle isoforms of tropomyosin / V. Nefedova, M. Marchenko, S. Kleymenov et al. // Biochemical and Biophysical Research Communications. — 2019. — Vol. 514, no. 3. — P. 613–617. Tropomyosin (Tpm) is an α-helical coiled-coil protein dimer, which forms a continuous head-to-tail polymer along the actin filament. In striated muscles, Tpm plays an important role in the Ca2+-dependent regulation of muscle contraction. However, little is known about functional and especially structural properties of the numerous non-muscle Tpm isoforms. In the present work, we have applied circular dichroism (CD) and differential scanning calorimetry (DSC) to investigate thermal unfolding and domain structure of various non-muscle human Tpm isoforms. These isoforms, the products of two different genes, TPM1 and TPM3, also significantly differ by alternatively spliced exons: N-terminal exons 1a2b or 1b, internal exons 6a or 6b, and C-terminal exons 9a, 9c or 9d. Our results clearly demonstrate that structural properties of various non-muscle Tpm isoforms can be quite different depending on the presence of different alternatively spliced exons in their genes. These data show for the first time a significant difference in the thermal unfolding between muscle and non-muscle Tpm isoforms and indicate that replacement of alternatively spliced exons alters the stability of certain domains in the Tpm molecule. [ DOI ]

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