Fundamentals of Protein Folding

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Book Chapter

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Data accumulated to date suggest that a protein can exist in at least three global forms: functional and folded, functional and intrinsically disordered, and nonfunctional and misfolded or aggregated. Therefore, in in vitro experiments or in the cellular environment, a polypeptide chain faces a choice among three potential routes: nonfolding, folding, and misfolding, with the last two representing competitive routes to higher structural order. This chapter covers several protein folding–related problems, such as a protein-folding code; major models of protein folding; polymer aspects underlying protein folding and structural peculiarities of the unfolded state and folding intermediates; and peculiarities of protein amino acid compositions favoring formation of equilibrium partially folded intermediate. All the functional and structural peculiarities of intrinsically disordered proteins (IDPs) and IDP regions (IDPRs) are encoded in their amino acid sequences. Data have been reported indicating that the critical step in protein fibrillogenesis is partial unfolding of the protein.

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Fundamentals of Protein Folding, in S. M. Doglia & M. Lotti (Eds.), Protein Aggregation in Bacteria: Functional and Structural Properties of Inclusion Bodies in Bacterial Cells, John Wiley & Sons, p. 1-62