Structural studies on histones H1. Circular dichroism and difference spectroscopy of the histones H1 and their trypsin-resistant cores from calf thymus and from the fruit fly Ceratitis capitata

Biochemistry ◽  
1980 ◽  
Vol 19 (17) ◽  
pp. 4080-4087 ◽  
Author(s):  
Jose L. Barbero ◽  
Luis Franco ◽  
Francisco Montero ◽  
Federico Moran
Keyword(s):  
Circular Dichroism ◽  
Ceratitis Capitata ◽  
Fruit Fly ◽  
Structural Studies ◽  
Difference Spectroscopy ◽  
Calf Thymus ◽  
Circular Dichroïsm

Circular dichroism studies of calf thymus Ca2+nucleohistone IV

Biochemistry ◽  
1972 ◽  
Vol 11 (8) ◽  
pp. 1431-1436 ◽  
Author(s):  
Thomas E. Wagner ◽  
Vaughn Vandegrift
Keyword(s):  
Circular Dichroism ◽  
Calf Thymus ◽  
Circular Dichroïsm

The thermal denaturation of bovine cardiac G-actin

1977 ◽  
Vol 55 (4) ◽  
pp. 325-331 ◽  
Author(s):  
C. C. Contaxis ◽  
C. C. Bigelow ◽  
C. G. Zarkadas
Keyword(s):  
Circular Dichroism ◽  
Conformational Change ◽  
Thermodynamic Analysis ◽  
Thermal Denaturation ◽  
State Transition ◽  
Thermal Unfolding ◽  
Difference Spectroscopy ◽  
Maximum Stability ◽  
Ph Range ◽  
Circular Dichroïsm

The thermal denaturation of bovine cardiac G-actin has been studied by ultraviolet difference spectroscopy and circular dichroism between pH 7.5 and 10.5. As with proteins previously studied, thermal unfolding is incomplete compared with unfolding by urea or GuHCl. However, the same conformational change is observed over the pH range studied, and the available evidence indicates it is a two-state transition. Thermodynamic analysis of the data shows that ΔH0 and ΔS0 are strongly dependent on the temperature, that ΔCp is 1300 cal deg−1 mol−1, and that G-actin has a temperature of maximum stability near −5 °C.

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