The energetics of T4 lysozyme reveal a hierarchy of conformations

Manuel Llinas, Blake Gillespie, Frederick W. Dahlquist, Susan Marqusee

Research output: Contribution to journalArticlepeer-review

103 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1072-1078
Number of pages7
JournalNature Structural Biology
Volume6
Issue number11
DOIs
StatePublished - 1999

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Genetics

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