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Temperature stability of proteins: Analysis of irreversible denaturation using isothermal calorimetry
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Outgoing claims: the papers this work cites, builds on, or argues with.
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Enzyme Kinetics Determined Using Calorimetry: A General Assay for Enzyme Activity?
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Challenges in the Development of High Protein Concentration Formulations
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[14]Determination and analysis of urea and guanidine hydrochloride denaturation curves
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Ligand binding analysis and screening by chemical denaturation shift
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Denatured state aggregation parameters derived from concentration dependence of protein stability
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Reversible and irreversible unfolding of multi-domain proteins
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Analysis of differential scanning calorimetry data for proteins Criteria of validity of one-step mechanism of irreversible protein denaturation
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Advancements in High Throughput Biophysical Technologies: Applications for Characterization and Screening during Early Formulation Development of Monoclonal Antibodies
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Trends in isothermal microcalorimetry
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Hydrophobic effect in protein folding and other noncovalent processes involving proteins.
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Calorimetric Determination of Thermodynamic Parameters of Reaction Reveals Different Enthalpic Compensations of the Yeast Hexokinase Isozymes
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A comparison of biophysical characterization techniques in predicting monoclonal antibody stability
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THE RESEARCH OF THE TYPES OF MOISTURE BONDS IN PROTEIN-CARBOHYDRATE CONCENTRATES OF CHEESE WHEY
inferred← citeshttps://doi.org/10.70675/a6794100zcc61z4406zb882za4f8f4b23e3bopenalex-snapshot
Caractérisation d'une protéine à domaine J impliquée dans l'adaptation à la basse température chez Shewanella oneidensis
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