Physical-chemical characterization and stability study of α-trypsin at pH 3.0 by differential scanning calorimetry-Reference-Cited by-同舟云学术

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Physical-chemical characterization and stability study of α-trypsin at pH 3.0 by differential scanning calorimetry

Published:2008-04 Issue:3 Volume:42 Page:278-284
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Santos A.M.C.,Santana M.A.,Gomide F.T.F.,Miranda A.A.C.,Oliveira J.S.,Boas F.A.S. Vilas,Vasconcelos A.B.,Bemquerer M.P.,Santoro M.M.

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference30 articles.

1. Thermodynamics of protein denaturation. Calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximation

2. A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study

3. [2]Scanning microcalorimetry in studying temperature-induced changes in proteins

4. Thermodynamic Problems of Protein Structure

5. Pseudotrypsin

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3. Evaluation of biological activities, structural and conformational properties of bovine beta- and alpha-trypsin isoforms in aqueous-organic media;International Journal of Biological Macromolecules;2021-04

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