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Context is a major determinant of β-sheet propensity

Nature volume 371, pages 264–267 (1994)Cite this article

Abstract

RESIDUES in β-sheets occur in two distinct tertiary contexts: central strands, bordered on both sides by other β-strands, and edge strands, bordered on only a single side by another β-strand1. The ΔΔG values for β-sheet formation measured at an edge β-strand of the IgG-binding domain of protein G(GB1) are quite different from those obtained previously2,3 at a central position in the same protein. In particular, there is no correlation at the edge position with statistically determined β-sheet-forming preferences4. The differences between β-sheet propensities measured at central and edge β-strands, ΔΔΔG values, correlate with the values of water/octanol transfer free energies5 and side-chain non-polar surface area for the amino acids6. These results strongly suggest that, unlike α-helix formation, β-sheet formation is determined in large part by tertiary context, even at solvent-accessible sites, and not by intrinsic secondary structure preferences.

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Authors and Affiliations

  1. Department of Chemistry, Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Nine Cambridge Center, Cambridge, Massachusetts, 02142, USA

    Daniel L. Minor Jr

  2. Department of Biology, Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Nine Cambridge Center, Cambridge, Massachusetts, 02142, USA

    Peter S. Kim

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  1. Daniel L. Minor Jr
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Minor, D., Kim, P. Context is a major determinant of β-sheet propensity. Nature 371, 264–267 (1994). https://doi.org/10.1038/371264a0

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