He said hydrophobic effects in protein folding have been recognized since the 1940s. "It's a rather tricky thing, though, because it has unusual temperature dependencies," Pratt said.

The folding patterns are pre-programmed for each protein, and the folded structures are designed to enable specific interactions with other molecules for specific functions.

In the work presented here, we have analyzed the effect on protein folding kinetics of >40 different amino acid substitutions at nine positions in the hydrophobic core of the Fyn tyrosine kinase ...

Proteins are the workers, messengers, managers, and directors of nearly all inter- and intra-cellular functions in our body. So, all advances in biology, pharmaceuticals, and related fields hinge ...

It's a long-standing assumption that the presence of water influences how proteins fold. A new study is challenging the details. A paper in the American Chemical Society's Journal of Physical ...

Physical Chemistry Chemical Physics, n°16 (01agosto2014)Onofrio Angelo - Department of Biosciences, Biotechnologies and Biopharmaceutics, University of Bari, Via ...

Levinthal noted that the chemical bonds of proteins give them tremendous freedom to adopt countless configurations—he estimated that a typical protein could exist in up to 10 300 configurations.

He said hydrophobic effects in protein folding have been recognized since the 1940s. "It's a rather tricky thing, though, because it has unusual temperature dependencies," Pratt said.