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Nat Struct Biol. 1999 Nov;6(11):1072-8.

The energetics of T4 lysozyme reveal a hierarchy of conformations.

Author information

1
Department of Molecular and Cell Biology, 229 Stanley Hall, University of California, Berkeley, Berkeley, California 94720, USA.

Abstract

We have used native state exchange to examine the energy landscape of the well-characterized protein T4 lysozyme. Although the protein exhibits two-state behavior by traditional probes, the energy landscape determined here is much more complex. The average stability of the C-terminal subdomain is significantly higher than that for the N-terminus suggesting at least two regions of unfolding. At a more detailed level, there appears to be a broad continuum of stabilities throughout each region. The overall subdomain hierarchy of energies does not mirror data on the folding pathway for this protein, challenging the relationship between energy landscapes and folding trajectories.

PMID:
10542101
DOI:
10.1038/14956
[Indexed for MEDLINE]

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