Abstract
Thermodynamics concerning the interaction of the bovine basic pancreatic trypsin inhibitor as well as bovine and porcine pancreatic secretory trypsin inhibitor with some serine (pro)enzymes has been obtained at pH 8.0 (I = 0.1 M) between 5 °C and 45 °C. Results have been analyzed by the enthalpy-entropy compensation plot (ΔHo ° versus ΔSo) and linear relationships obtained, suggesting the involvment of protein conformation and possibly hydration in the process(es) of protein-protein interaction(s).
| Original language | English |
|---|---|
| Pages (from-to) | 177-180 |
| Number of pages | 4 |
| Journal | Advances in the Biosciences |
| Volume | 65 |
| Issue number | C |
| Publication status | Published - 1987 |
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Keywords
- (pro)enzyme:inhibitor complexes
- enthalpy-entropy compensation phenomena
- macromolecular inhibitors
- Serine (pro)enzymes
- thermodynamics
Cite this
Enthalpy-entropy compensation phenomena in serine (Pro) enzyme : Inhibitor complex formation. / Amiconi, G.; Ascenzi, P.; Bolognese, M.; Guarneri, M.; Menegatti, E.
In: Advances in the Biosciences, Vol. 65, No. C, 1987, p. 177-180.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Enthalpy-entropy compensation phenomena in serine (Pro) enzyme
T2 - Inhibitor complex formation
AU - Amiconi, G.
AU - Ascenzi, P.
AU - Bolognese, M.
AU - Guarneri, M.
AU - Menegatti, E.
PY - 1987
Y1 - 1987
N2 - Thermodynamics concerning the interaction of the bovine basic pancreatic trypsin inhibitor as well as bovine and porcine pancreatic secretory trypsin inhibitor with some serine (pro)enzymes has been obtained at pH 8.0 (I = 0.1 M) between 5 °C and 45 °C. Results have been analyzed by the enthalpy-entropy compensation plot (ΔHo ° versus ΔSo) and linear relationships obtained, suggesting the involvment of protein conformation and possibly hydration in the process(es) of protein-protein interaction(s).
AB - Thermodynamics concerning the interaction of the bovine basic pancreatic trypsin inhibitor as well as bovine and porcine pancreatic secretory trypsin inhibitor with some serine (pro)enzymes has been obtained at pH 8.0 (I = 0.1 M) between 5 °C and 45 °C. Results have been analyzed by the enthalpy-entropy compensation plot (ΔHo ° versus ΔSo) and linear relationships obtained, suggesting the involvment of protein conformation and possibly hydration in the process(es) of protein-protein interaction(s).
KW - (pro)enzyme:inhibitor complexes
KW - enthalpy-entropy compensation phenomena
KW - macromolecular inhibitors
KW - Serine (pro)enzymes
KW - thermodynamics
UR - http://www.scopus.com/inward/record.url?scp=0013471307&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0013471307&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0013471307
VL - 65
SP - 177
EP - 180
JO - Advances in the Biosciences
JF - Advances in the Biosciences
SN - 0065-3446
IS - C
ER -