[Study of thermal denaturation of the rod part of myosin molecule by microcalorimetry and intrinsic fluorescence methods].
Thermal denaturation of myosin rod has been studied by differential scanning microcalorimetry and intrinsic tryptophane fluorescence methods. Use of the sequence annealing in the calorimetric measurement allows to decompose the total thermogram of rod into four elementary bands with maxima at 42, 46.5, 50 and 57 degrees C. Fluorescence changes occur at temperatures which coincide with the first, second and fourth calorimetric peaks. Changes of the time resolved and steady state fluorescence of myosin rod were interpreted using the data on localization of tryptophan residues in the molecule. The tryptophan fluorescence of myosin rod is assumed to monitor the denaturational changes in high meromyosin and probably in the hinge region but not in the subfragment 2.
Shnyrov
V L
VL
Vedenkina
N S
NS
Ostrovskiĭ
A V
AV
Permiakov
E A
EA
Golitsyna
N L
NL
Levitskiĭ
D I
DI
D000818:Animals; D002152:Calorimetry, Differential Scanning; D006358:Hot Temperature; D009132:Muscles / Q000737:chemistry; D009218:Myosins; D011487:Protein Conformation; D011489:Protein Denaturation; D011817:Rabbits; D013050:Spectrometry, Fluorescence; D014364:Tryptophan
D014364:Tryptophan; D009218:Myosins
Issledovanie teplovoĭ denaturatsii sterzhnevoĭ chasti molekuly miozina metodami mikrokalorimetrii i sobstvennoĭ fluorestsentsii.