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A fluorescence stopped-flow kinetic study of the conformational activation of α-chymotrypsin and several mutants

The kinetic activation parameters (activation free energy, activation free enthalpy, and activation free entropy change) of the conformational change of α-chymotrypsin from an inactive to the active conformation were determined after a pH jump from pH 11.0 to pH 6.8 by the fluorescence stopped-flow...

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Detaylı Bibliyografya
Asıl Yazarlar: Verheyden, Gert, Matrai, Janka, Volckaert, Guido, Engelborghs, Yves
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: Cold Spring Harbor Laboratory Press 2004
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC2280002/
https://ncbi.nlm.nih.gov/pubmed/15322291
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.04709604
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