To use all functions of this page, please activate cookies in your browser.
With an accout for my.chemeurope.com you can always see everything at a glance – and you can configure your own website and individual newsletter.
- My watch list
- My saved searches
- My saved topics
- My newsletter
Hydrophobic collapse is a hypothesized event that occurs during the folding process of globular proteins, suggested on the basis of the observation that proteins' native states often contain a hydrophobic core of nonpolar amino acid side chains (interspersed with charged side chains that are neutralized by salt bridges) in the protein's interior, leaving most of the polar or charged residues on the solvent-exposed protein surface. The energetic stabilization conferred on the protein by the sequestration of the hydrophobic side chains from the surrounding water is thought to stabilize folding intermediates. The hypothesis generally posits that hydrophobic collapse is relatively early event in the folding pathway, occurring before the formation of many secondary structures and native contacts present in the fully folded tertiary structure. The collapsed intermediate is also referred to as a molten globule and corresponds to a partially folded state whose energy is lower than that of the denatured state but higher than that of the native state - that is, within the energy well of the folding funnel but not yet close to the energy minimum.
Additional recommended knowledge
Partial hydrophobic collapse is an experimentally accepted model for the folding kinetics of many globular proteins, such as myoglobin, alpha-lactalbumin, barstar, and staphylococcal nuclease. However, because experimental evidence of early folding events is difficult to obtain, hydrophobic collapse is often studied in silico via molecular dynamics and Monte Carlo simulations of the folding process. Globular proteins that are thought to fold by hydrophobic collapse are particularly amenable to complementary computational and experimental study using phi value analysis.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Hydrophobic_collapse". A list of authors is available in Wikipedia.|