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Compact Intermediates States in Protein Folding

  • Chapter
Proteins: Structure, Function, and Engineering

Part of the book series: Subcellular Biochemistry ((SCBI,volume 24))

Abstract

Recently there has been growing recognition of the existence and importance of compact intermediate states of proteins. Such species have been observed under both transient (refolding kinetics) and equilibrium conditions. It is clear that for many proteins most denaturing conditions do not lead to a fully unfolded protein (random coil), but rather to species with substantial secondary structure and substantial compactness, relative to the fully unfolded state. In addition, there is now good experimental data to demonstrate the existence of two classes of compact denatured states of proteins: compact intermediates, in the thermodynamic sense (i.e., a minimum in the free energy profile for the reaction), and compact substates of the unfolded state (Palleros et al., 1993). It is important to note that it is often experimentally difficult to distinguish between these two types of compact denatured states, especially by spectral methods. Recent reviews of compact denatured states, and particularly the molten globule, include those of Dill and Shortle (1991), Ptitsyn (1987, 1992), Kuwajima (1989), Christensen and Pain (1991), and Baldwin and Roder (1991). Theoretical models for the existence of two classes of denatured states have been presented by Dill and co-workers (Alonso et al., 1991), Ptitsyn (1987, 1992), and Finkelstein and Shakhnovich (1989).

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Authors and Affiliations

  1. Department of Chemistry and Biochemistry, University of California, Santa Cruz, California, 95064, USA

    Anthony L. Fink

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  1. Anthony L. Fink
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  1. Department of Biophysics, Bose Institute, Calcutta, 700054, India

    B. B. Biswas  & Siddhartha Roy  & 

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© 1995 Springer Science+Business Media New York

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Fink, A.L. (1995). Compact Intermediates States in Protein Folding. In: Biswas, B.B., Roy, S. (eds) Proteins: Structure, Function, and Engineering. Subcellular Biochemistry, vol 24. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1727-0_2

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  • DOI: https://doi.org/10.1007/978-1-4899-1727-0_2

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  • Print ISBN: 978-1-4899-1729-4

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