pH titration of native and unfolded ß-trypsin: evaluation of the D D G0 titration and the carboxyl pK values
The stabilizing free energy of ß-trypsin was determined by hydrogen ion titration. In the pH range from 3.0 to 7.0, the change in free energy difference for the stabilization of the native protein relative to the unfolded one (<!-- $MVD$:face("Symbol") -->D D G0 titration) was 9.51 ±...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
Associação Brasileira de Divulgação Científica
1997-11-01
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| Series: | Brazilian Journal of Medical and Biological Research |
| Subjects: | |
| Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997001100003 |