| Registro completo |
| Provedor de dados: |
BJMBR
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| País: |
Brazil
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| Título: |
pH titration of native and unfolded ß-trypsin: evaluation of the D D G0 titration and the carboxyl pK values
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| Autores: |
Günther,A.R.
Santoro,M.M.
Rogana,E.
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| Data: |
1997-11-01
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| Ano: |
1997
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| Palavras-chave: |
SS-trypsin
Protein stability
Protein pH titration
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| Resumo: |
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 ± 0.06 kcal/mol. An isoelectric point of 10.0 was determined, allowing us to calculate the Tanford and Kirkwood electrostatic factor w. This factor presented a nonlinear behavior and indicated more than one type of titratable carboxyl groups in ß-trypsin. In fact, one class of carboxyl group with a pK = 3.91 ± 0.01 and another one with a pK = 4.63 ± 0.03 were also found by hydrogen ion titration of the protein in the folded state
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| Tipo: |
Info:eu-repo/semantics/article
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| Idioma: |
Inglês
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| Identificador: |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997001100003
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| Editor: |
Associação Brasileira de Divulgação Científica
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| Relação: |
10.1590/S0100-879X1997001100003
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| Formato: |
text/html
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| Fonte: |
Brazilian Journal of Medical and Biological Research v.30 n.11 1997
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| Direitos: |
info:eu-repo/semantics/openAccess
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