Exploring the conformational energy landscape of proteins

G. Ulrich Nienhaus, Joachim D. Müller, Ben H. McMahon, Hans Frauenfelder

Research output: Contribution to journalArticlepeer-review

80 Scopus citations

Abstract

Proteins possess a complex energy landscape with a large number of local minima called conformational substates that are arranged in a hierarchical fashion. Here we discuss experiments aimed at the elucidation of the energy landscape in carbonmonoxy myoglobin (MbCO). In the highest tier of the hierarchy, a few taxonomic substates exist. Because of their small number, these substates are accessible to detailed structural investigations. Spectroscopic experiments are discussed that elucidate the role of protonations of amino acid side chains in creating the substates. The lower tiers of the hierarchy contain a large number of statistical substates. Substate interconversions are observed in the entire temperature range from below 1 K up to the denaturation temperature, indicating a wide spectrum of energy barriers that separate the substates.

Original languageEnglish (US)
Pages (from-to)297-311
Number of pages15
JournalPhysica D: Nonlinear Phenomena
Volume107
Issue number2-4
DOIs
StatePublished - 1997
Externally publishedYes

Bibliographical note

Funding Information:
This work was supported by grants GM 18051 from the National Institutes of Health and PHY95-13217 from the National Science Foundation.

Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.

Keywords

  • Conformational substates
  • Energy landscape
  • Infrared spectroscopy
  • Myoglobin
  • Protein dynamics

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