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A study of the hydration of ribonuclease A using isothermal calorimetry: Effect of the protein hydrophobicity and polarity to find the excess thermodynamic functions of binary protein-water systems. Isothermal calorimetry
Analysis of hydration of ovalbumin by isothermal calorimetry to characterize the hydration dependencies of the excess thermodynamic functions of binary proteinwater systems
Analysis of hydration of binary protein-water mixtures. methodology principles of a novel methodology to investigate the protein-water interactions. This methodology is based
A study of the hydration of ribonuclease A using isothermal calorimetry: Effect of the protein hydrophobicity and polarity to find the excess thermodynamic functions of binary protein-water systems. Isothermal calorimetry
Participation of Septin Cytoskeletal Proteins in the Nervous System Functioning and their biological functions. An increasing number of studies show that these proteins play an important role
Cloning, expression, and purification of the nucleocapsid protein of SARS coronavirusCloning, expression, and purification of the nucleocapsid protein of SARS coronavirus
Entropy Analysis of Protein Sequences Reveals a Hierarchical Organization, and the study of the mechanisms of functioning of protein molecular machines are given. Conclusions: ANIS method
Analysis of hydration of ovalbumin by densitometry of ovalbumin with water were obtained as a function of composition at 25 °C. The hydration process
Protein - water interactions: A differential approach which molecular parameters control the thermodynamics, structure, and functions of the protein
Protein - water interactions: A differential approach which molecular parameters control the thermodynamics, structure, and functions of the protein
Страница 2 из 4765
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