Abstract
With the growing body of knowledge of protein structure has come the realization that proteins are not rigid, inflexible structures. Rather their structures are dynamic and are characterized by marginal stability and conformational equilibria. Their structures represent a minimization of the sum of the free energies resulting from noncovalent interactions between amino acid residues within a polypeptide chain, between residues in contacting polypeptide chains, and between residues and solvent molecules. Because of their marginal stability, protein structures are sensitive to environmental change and alteration in their structure may be reversible or irreversible. Neglecting postsynthetic covalent change, proteins will refold to their native conformation from a random coil state under conditions which mimic the physiological environment. This result is a consequence of the thermodynamic nature of their structural stabilization. Recent evidence suggests that folding pathways as well as the native structures are determined by the primary structure and the consequent thermodynamics of noncovalent interactions between residues and residues plus solvent [1].
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© 1989 Dr. Dietrich Steinkopff Verlag GmbH & Co. KG, Darmstadt
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Swaisgood, H.E. (1989). Structural Changes in Milk Proteins. In: Barth, C.A., Schlimme, E. (eds) Milk Proteins. Steinkopff. https://doi.org/10.1007/978-3-642-85373-9_30
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DOI: https://doi.org/10.1007/978-3-642-85373-9_30
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