Stability of two beta-tropomyosin isoforms: effects of mutation Arg91Gly.
In order to comprehend the domain structure of two beta-tropomyosin (beta-Tm) isoforms (skeletal muscle and smooth muscle beta-Tm) and the influence of the disease-causing mutation Arg91Gly on it, we studied the thermal unfolding of these tropomyosin species by means of differential scanning calorim...
Main Authors: | Nevzorov, I, Redwood, C, Levitsky, D |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2008
|
Similar Items
-
Effect of mutation Arg91Gly on the thermal stability of β-tropomyosin
by: Nevzorov, I, et al.
Published: (2008) -
[Effect of mutation Arg9lGly on the thermal stability of beta-tropomyosin]
by: Nevzorov, I, et al.
Published: (2008) -
Gly126Arg substitution causes anomalous behaviour of α-skeletal and β-smooth tropomyosins during the ATPase cycle.
by: Rysev, N, et al.
Published: (2014) -
The effect of the arthrogryposis-causing Arg91Gly mutation in beta-skeletal tropomyosin on its position on the thin filament and flexibility during the ATPase cycle
by: Simonyan, A, et al.
Published: (2013) -
Conserved noncanonical residue Gly-126 confers instability to the middle part of the tropomyosin molecule.
by: Nevzorov, I, et al.
Published: (2011)