Journal
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
Volume 30, Issue 1, Pages 113-124Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2012.674286
Keywords
protein folding; hydrophobic; hydrophilic effects; hydrophilic forces; Anfinsen's hypothesis; Levinthal's question
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Attempts to answer the Levinthal question How proteins fold to give such a unique structure are discussed. In the first part of this article, we focus on a few reasons as to why the solution to the protein-folding problem (PFP) has been elusive for a very long time. One is a result of the misinterpretation of Anfinsen's Thermodynamic hypothesis which led to the conclusion that the native structure of a protein must be at a global minimum of the Gibbs energy. The second is the result of the adherence to the hydrophobic paradigm, and at the same time ignoring a whole repertoire of hydrophilic effects. It is argued that switching from a target-based to a caused-based approach, and adopting the hydrophilic paradigm leads straightforwardly to a simple answer to Levinthal's question, as well as to a solution of the PFP.
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