DSC studies of the conformational stability of barstar wild-type

Schöppe, Arnulf ; Hinz, Hans-Jürgen ; Agashe, Vishwas R. ; Ramachandran, S. ; Udgaonkar, Jayant B. (1997) DSC studies of the conformational stability of barstar wild-type Protein Science, 6 (10). pp. 2196-2202. ISSN 0961-8368

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Official URL: http://onlinelibrary.wiley.com/doi/10.1002/pro.556...

Related URL: http://dx.doi.org/10.1002/pro.5560061014


The temperature induced unfolding of barstar wild-type of bacillus amyloliquefaciens (90 residues) has been characterized by differential scanning microcalorimetry. The process has been found to be reversible in the pH range from 6.4 to 8.3 in the absence of oxygen. It has been clearly shown by a ratio of δHvH/δHcal near 1 that denaturation follows a two-state mechanism. For comparison, the C82A mutant was also studied. This mutant exhibits similar reversibility, but has a slightly lower transition temperature. The transition enthalpy of barstar wt (303 kJ mol−1) exceeds that of the C82A mutant (276 kJ mol−1) by approximately 10%. The heat capacity changes show a similar difference, δCp being 5.3+1 kJ mol−1 K−1 for the wild-type and 3.6 δ 1 kJ mol−1 K−1 for the C82A mutant. The extrapolated stability parameters at 25 ° C are δG°=23.5+2 kJ mol−1 for barstar wt and δG0=25.5+2 kJ mol−1 for the C82A mutant.

Item Type:Article
Source:Copyright of this article belongs to Cold Spring Harbor Laboratory Press.
Keywords:Aggregation Prevention; Barstar Wild-type; DSC; Oxidization; Thermodynamics
ID Code:54319
Deposited On:11 Aug 2011 12:13
Last Modified:11 Aug 2011 12:13

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