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The thermodynamic stability of pancreatic ribonuclease B (RNase B), which possesses identical protein structure of pancreatic ribonuclease A (RNase A), but differs by the presence of a carbohydrate chain attached to Asn 34, was studied by means of di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______3730::cf327575ad87c70eb7c52f2756629ffa
http://hdl.handle.net/11588/139878
http://hdl.handle.net/11588/139878
The thermal denaturation of S-protein is investigated at pH 7.0 by means of DSC measurements. The process is reversible and can be assimilated to a two-state transition. The low values of denaturation temperature and enthalpy, between 38.5 and 40.0
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______3730::a90bc5a006ed735c22a216e3d603940c
http://hdl.handle.net/11588/145763
http://hdl.handle.net/11588/145763