Spectral diffusion and the energy landscape of a protein.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 8986777.
- Also identified by PMC identifier 26370.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
Abstract
We present a novel type of spectral diffusion experiment in the millikelvin range to characterize the energy landscape of a protein as compared with that of a glass. We measure the time evolution of spectral holes for more than 300 hr after well-defined initial nonequilibrium conditions. We show that the model of noninteracting two-level systems can describe spectral diffusion in the glass, but fails for the protein. Our results further demonstrate that randomness in the energy landscape of a protein shows features of organization. There are "deep minimum" states separated by barriers, the heights of which we are able to estimate. The energy landscape of a glass is featureless by comparison.
Medical subject headings
- Models, Structural
- Myoglobin
- Protein Conformation
- Proteins