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- W2064274321 abstract "The state of proteins in water-protein systems was investigated qualitatively using viscosimetric technique and preparative ultracentrifugation. In the case of cooperative processes, 4 concentration intervals bounded by three critical concentrations have been found for each protein.The first value of critical concentration is bound up with the initiation of supermolecular formations (herein also referred to as associates) due to self-association of polypeptide chains. The second critical concentration is observed when the weight fraction of associate becomes predominant (80–85%) and when the change of secondary and tertiary structures is completed.The third critical concentration is connected with the change in the nature of supermolecular formations.The thermodynamic stability of the water-protein system varies when the critical concentrations are passed through. The system is stable and, apparently, close to the true solution over the first concentration interval. As soon as the first critical concentration is reached, colloid particles appear in the system and become predominant after the second critical concentration is passed, and the solution should be considered as a colloid one." @default.
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- W2064274321 date "1984-01-01" @default.
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- W2064274321 title "Structure of protein solutions. Part 1. Investigation and interpretation of viscosity anomalies" @default.
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- W2064274321 doi "https://doi.org/10.1002/food.19840280502" @default.
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