The protein folded and unfolded, with the results closely matching experimental data.

The mechanisms by which proteins fold are not completely known.

After synthesis, proteins typically fold into a particular three-dimensional conformation: their native state.

This means that proteins may not fold completely in either transient or permanent complexes.

If proteins do not fold into their native shape, they are inactive and are usually toxic.

Still, given other information, such as how proteins with similar sequences fold, scientists have used computers to make intelligent guesses.

In addition, scientists believe that proteins should fold into the most stable shape, the one with the lowest thermodynamic energy level.

Locally stabilized structures would reduce the search space and allow proteins to fold on the order of milliseconds.

Under some conditions proteins will not fold into their biochemically functional forms.

Why should natural proteins fold in a way that scientists will find easy to predict?