Energy landscape in protein folding and unfolding.
basic_science · Level V
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- Record sourced from PubMed, PMID 26957601.
- Also identified by DOI 10.1073/pnas.1524864113 and PMC identifier 4812744.
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Abstract
We use (1)H NMR to probe the energy landscape in the protein folding and unfolding process. Using the scheme ⇄ reversible unfolded (intermediate) → irreversible unfolded (denatured) state, we study the thermal denaturation of hydrated lysozyme that occurs when the temperature is increased. Using thermal cycles in the range 295 < T < 365 K and following different trajectories along the protein energy surface, we observe that the hydrophilic (the amide NH) and hydrophobic (methyl CH3 and methine CH) peptide groups evolve and exhibit different behaviors. We also discuss the role of water and hydrogen bonding in the protein configurational stability.
Medical subject headings
- Protein Folding