Correct folding requires proteins to assume one particular structure from a constellation of possible but incorrect conformations.

These fractional assignments place important constraints on the possible secondary conformations that the protein can be in.

In this way, data about various possible conformations of a tripeptide is gathered and analyzed as explained in the discussion section.

For example, n-butane has two possible conformations, anti and gauche.

However, there are two possible gauche conformations and only one anti conformation.

More complex molecules, such as butane, have more than one possible staggered conformation.

The possible different conformations of these Kv1.3 and 1.5 complexes can affect the immune response.

In any short sequence, the molecular forces constrain the structure, leading to only a small number of possible conformations, which can be modeled by fragments.

Examining the entire crystallized data will give the other possible conformations of the tripeptide structures in proteins.

Many of these possible conformations have nearly the same energy that results from stearic repulsion.