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 language | English (US) |
|---|---|
| Pages (from-to) | 297-311 |
| Number of pages | 15 |
| Journal | Physica D: Nonlinear Phenomena |
| Volume | 107 |
| Issue number | 2-4 |
| DOIs | |
| State | Published - 1997 |
| Externally published | Yes |
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.
Keywords
- Conformational substates
- Energy landscape
- Infrared spectroscopy
- Myoglobin
- Protein dynamics