Table 2 Monomer-dimer and Trp43 conformational exchange activation energies.

From: Origin of conformational dynamics in a globular protein

Sequence

Peaks

Eaapp1→2a (kcal/mol)

Eaapp2→1b (kcal/mol)

Arrhenius behaviorc

WT-A34F

W43ε

8 ± 1

10 ± 2

Yes

T17

10 ± 1

12 ± 1

Yes

D3-L39V

W43ε

19 ± 2

16 ± 2

Yes

T17

18 ± 2

17 ± 2

Yes

DANCER-3

W43ε

9 ± 1

−27 ± 3

No

T17

7 ± 1

12 ± 1

Yes

D3-F3Y

W43ε

3 ± 1

1.6 ± 0.3

Yesd

T17

13 ± 1

16 ± 2

Yes

D3-I7L

W43εe

N/A

N/A

N/A

T18

31 ± 3

25 ± 2

Yes

D3-I54V

W43ε

0f

0f

Nod

T17

8 ± 2

12 ± 1

Yes

WT-A34F/V39L

W43ε

1.6 ± 0.2

−4.7 ± 0.6

No

T18

9 ± 1

13 ± 1

Yes

  1. aApparent activation energy for exchange from the major state (the most populated state at the lowest temperature tested) to the minor state (the least populated state at the lowest temperature tested) (n = 2 analytical replicates, mean ± s.d.)
  2. bApparent activation energy for exchange from the minor state to the major state (n = 2 analytical replicates, mean ± s.d.)
  3. cArrhenius behavior is defined here as a positive activation energy for both transitions
  4. dAlthough D3-F3Y activation energies are both positive, they are weak compared to T17 (Supplementary Fig. 10). It is expected that for one process, they would be similar. This is not the case, thus different dynamic processes are being sensed by D3-F3Y Trp43ε and T17
  5. eW43ε minor state peaks and crosspeaks could not be quantified for D3-I7L but are present
  6. fExchange rates did not vary as a function of temperature over the range measured
Back to article page