Range |
Table - link
|
Organism |
Bacteria Escherichia coli |
Reference |
Turner L, Caplan SR, Berg HC. Temperature-induced switching of the bacterial flagellar motor. Biophys J. 1996 Oct71(4):2227-33. p.2231 table 1PubMed ID8889199
|
Method |
"[Researchers] used a strain of Escherichia coli (HCB437) that lacks
chemotaxis signaling proteins, including the response regulator
CheY, but which forms intact motor-switch complexes.
At room temperature, tethered cells of this strain spin exclusively CCW [counter clockwise]...[researchers] calculated the activation energies (Figs. 5 A and
B), enthalpies, and entropies (Figs. 6 A and B) for the
forward and reverse transitions for each cell from transition state theory ... The standard free energy
change was calculated from the equilibrium constant at
each temperature (Fig. 5 C), and the standard enthalpy
and entropy changes were calculated from the standard
free energy change as a function of temperature (Fig. 6
C)." |
Comments |
"The mean standard enthalpy and entropy changes for the
forward transition are, respectively, about -400 kJ/mol and -1.5 kJ/K mol (see Table 1)...Even though the values vary from cell to
cell, the overall trend is the same (Table 1). The standard
enthalpy and entropy changes and the forward activation
enthalpies and entropies are all negative the reverse
activation enthalpies and entropies are all positive." |
Entered by |
Uri M |
ID |
109868 |