A calorimetric study of pH-dependent thermal unfolding of leghemoglobin a from soybean
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference9 articles.
1. Characterization and improved separation of soybean leghemoglobins
2. Thermodynamic analysis of thermal transitions in globular proteins. I. Calorimetric study of ribotrypsinogen, ribonuclease and myoglobin
3. A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
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1. Meat and meat alternatives: where is the gap in scientific knowledge and technology?;Italian Journal of Animal Science;2023-05-16
2. pH-induced conformational isomerization of leghemoglobin from Arachis hypogea;Biochemistry (Moscow);2014-11
3. Amphiphile self-aggregation: An attempt to reconcile the agreement–disagreement between the enthalpies of micellization determined by the van’t Hoff and Calorimetry methods;Journal of Colloid and Interface Science;2009-09
4. Effect of Temperature on Hydrophobic Interaction between Proteins and Hydrophobic Adsorbents: Studies by Isothermal Titration Calorimetry and the van't Hoff Equation;Langmuir;2003-09-20
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