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Agnes Bolinska
University of South Carolina
  1. Successful visual epistemic representation.Agnes Bolinska - 2016 - Studies in History and Philosophy of Science Part A 56:153-160.
    In this paper, I characterize visual epistemic representations as concrete two- or three-dimensional tools for conveying information about aspects of their target systems or phenomena of interest. I outline two features of successful visual epistemic representation: that the vehicle of representation contain sufficiently accurate information about the phenomenon of interest for the user’s purpose, and that it convey this information to the user in a manner that makes it readily available to her. I argue that actual epistemic representation may involve (...)
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  2. Epistemic expression in the determination of biomolecular structure.Agnes Bolinska - 2023 - Studies in History and Philosophy of Science Part A 100 (C):107-115.
    Scientific research is constrained by limited resources, so it is imperative that it be conducted efficiently. This paper introduces the notion of epistemic expression, a kind of representation that expedites the solution of research problems. Epistemic expressions are representations that (i) contain information in a way that enables more reliable information to place the most stringent constraints on possible solutions and (ii) make new information readily extractible by biasing the search through that space. I illustrate these conditions using historical and (...)
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  3. A Monist Proposal: Against Integrative Pluralism About Protein Structure.Agnes Bolinska - 2022 - Erkenntnis 1 (4).
    Mitchell & Gronenborn propose that we account for the presence of multiple models of protein structure, each produced in different contexts, through the framework of integrative pluralism. I argue that two interpretations of this framework are available, neither of which captures the relationship between a model and the protein structure it represents or between multiple models of protein structure. Further, it inclines us toward concluding prematurely that models of protein structure are right in their contexts and makes extrapolation of findings (...)
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