Indirect effects can be the changing membrane potential or any perturbation that causes conformational change, which can change intermolecular forces between proteins.
Modeling this process requires a very accurate representation of not only intermolecular ion-channel and ion- water interactions, but also intramolecular channel-channel interactions.
Under these conditions polypeptides covalently linked by intermolecular disulphide bonds are displaced from the diagonal during the second-dimension electrophoresis.
Measurements on these samples provide quantitative constraints on intermolecular distances, torsion angles, or other aspects of amyloid fibril structures.
Complex formation with the chaperone thus allows the correction of misfolded conformations in an isolated environment without the danger of intermolecular aggregation reactions.
Thus, quaternary contacts can be either intermolecular or intramolecular.
Time-resolved measurements can, of course, equally well be used to study transitions linked to changes in intermolecular interactions.
A comparison is made to the dynamics of lubrication equations that include attractive and repulsive intermolecular interactions.
