Thermal unfolding of homodimers and heterodimers of different skeletal-muscle isoforms of tropomyosin

被引：17
|
作者：
Matyushenko, Alexander M. [1 ,2 ]
Kleymenov, Sergey Y. [1 ,3 ]
Susorov, Denis S. [1 ]
Levitsky, Dmitrii I. [1 ,4 ]
机构：
[1] Russian Acad Sci, Bach Inst Biochem, Res Ctr Biotechnol, Leninsky Prosp 33, Moscow 119071, Russia
[2] Russian Acad Sci, Inst Immunol & Physiol, Ekaterinburg 620049, Russia
[3] Russian Acad Sci, Koltzov Inst Dev Biol, Moscow 119334, Russia
[4] Moscow MV Lomonosov State Univ, Belozersky Inst Physicochem Biol, Moscow, Russia
来源：
BIOPHYSICAL CHEMISTRY | 2018年 / 243卷
基金：
俄罗斯科学基金会;
关键词：
Tropomyosin; Isoforms; Homodimers and heterodimers; Thermal unfolding; Differential scanning calorimetry; INTERCHAIN DISULFIDE BOND; ALPHA-TROPOMYOSIN; SMOOTH-MUSCLE; STABILITY; ACTIN; CARDIOMYOPATHY; FLUORESCENCE; EXPRESSION; MUTATIONS; RESIDUES;
D O I：
10.1016/j.bpc.2018.09.002
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
We applied differential scanning calorimetry (DSC) to investigate the structural properties of three isoforms of tropomyosin (Tpm), alpha, beta, and gamma, expressed from different genes in human skeletal muscles. We compared specific features of the thermal unfolding of alpha alpha, beta beta, and gamma gamma Tpm homodimers, as well as of alpha beta and gamma beta Tpm heterodimers. The results show that the thermal stability of gamma gamma homodimer is much higher than that of alpha alpha homodimer which, in turn, is much more thermostable than the beta beta homodimer. The stability of the gamma beta Tpm heterodimer is much lower than that of the gamma gamma homodimer, and its thermal unfolding is quite different from that for gamma gamma and beta beta homodimers, whereas the unfolding of the alpha beta heterodimer is roughly similar to that of the alpha alpha homodimer.
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页码：1 / 7
页数：7
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