<p>Proteins owe their diverse roles to their dynamic character. Two aspects of protein behavior that depend on dynamism are protein folding and conformational isomerization. While the former describes the process by which an unstructured polypeptide chain spontaneously folds into a protein with a specific three dimensional structure, the latter describes the reversible interconversion of distinct structural states of the protein. Apart from their scientific interest, protein folding and conformational isomerization raise important metaphysical questions concerning causation and identity. In this paper, I argue that protein folding is a dispositional teleological process in which the inherent potentiality of the unstructured polypeptide chain to fold into a specific three-dimensional form is manifested. Here, teleology is seen not as the end dictating the present, but the outworking of an entity’s potential. The conformational isomerization of a protein, and the existence of a protein not as a single structure but as an ensemble of conformational isomers, raises questions concerning identity – how should we conceive identity in the face of continuous change? To understand this, I propose a qualified meaning for ‘identity’ – dynamic identity, according to which change is recognized as an existential element of every actuality. All actualities are characterized by ceaseless activity, where this activity involves both an actuality’s internal, constitutive interactions as well as relationships with actualities in its environment. Combined, these internal and external relations act to maintain the actuality in a quasi-stable state while at the same time propelling the actuality into a future of transformation into other, successive quasi-stable states. An actuality’s activities not only sustain it in the present moment in a quasi-stable state, but also establish the conditions for progression into its future. This paper concludes by examining how the dynamic nature of proteins reveals fundamental metaphysical principles.</p>

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Metaphysics of protein dynamics: dispositional teleology and dynamic identity

  • Ross L. Stein

摘要

Proteins owe their diverse roles to their dynamic character. Two aspects of protein behavior that depend on dynamism are protein folding and conformational isomerization. While the former describes the process by which an unstructured polypeptide chain spontaneously folds into a protein with a specific three dimensional structure, the latter describes the reversible interconversion of distinct structural states of the protein. Apart from their scientific interest, protein folding and conformational isomerization raise important metaphysical questions concerning causation and identity. In this paper, I argue that protein folding is a dispositional teleological process in which the inherent potentiality of the unstructured polypeptide chain to fold into a specific three-dimensional form is manifested. Here, teleology is seen not as the end dictating the present, but the outworking of an entity’s potential. The conformational isomerization of a protein, and the existence of a protein not as a single structure but as an ensemble of conformational isomers, raises questions concerning identity – how should we conceive identity in the face of continuous change? To understand this, I propose a qualified meaning for ‘identity’ – dynamic identity, according to which change is recognized as an existential element of every actuality. All actualities are characterized by ceaseless activity, where this activity involves both an actuality’s internal, constitutive interactions as well as relationships with actualities in its environment. Combined, these internal and external relations act to maintain the actuality in a quasi-stable state while at the same time propelling the actuality into a future of transformation into other, successive quasi-stable states. An actuality’s activities not only sustain it in the present moment in a quasi-stable state, but also establish the conditions for progression into its future. This paper concludes by examining how the dynamic nature of proteins reveals fundamental metaphysical principles.