Table 4 Parameters resulting from fitting deconvoluted DSC thermograms (Fig. 6), averaged from at least three separate runs using CalFitter 1.2.

From: Thermostabilization of VPR, a kinetically stable cold adapted subtilase, via multiple proline substitutions into surface loops

Variant

Eact1

(kJ/mol)

Eact2

(kJ/mol)

ΔHcal-fit1

(kJ/mol)

ΔHcal-fit2

(kJ/mol)

VPR∆C

235 ± 2

N.A.

542 ± 5

N.A.

VPR∆C_N3P

251 ± 5

285 ± 20

318 ± 20

227 ± 19

VPR∆C_I5P

235 ± 3

356 ± 13

399 ± 7

180 ± 6

VPR∆C_N238P

248 ± 2

N.A.

564 ± 4

N.A.

VPR∆C_T265P

229 ± 2

N.A.

471 ± 5

N.A.

VPR∆C_N3P/I5P

261 ± 9

283 ± 6

176 ± 20

477 ± 19

VPR∆C_N3P/I5P/N238P

270 ± 11

279 ± 3

120 ± 13

567 ± 13

VPR∆C_N3P/I5P/T265P

259 ± 10

326 ± 8

224 ± 20

481 ± 18

VPR∆C_N3P/I5P/N238P/T265P

215 ± 8

383 ± 7

275 ± 17

425 ± 15

  1. Values shown are the activation energy (Eact) of unfolding transitions of PMSF inhibited VPR variants and ΔHcal-fit the calorimetric enthalpy of the fits. Numbers in superscript refer to the chronological order of transitions from the native to unfolded state. All values are represented with their 95% confidence interval.
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