Is tensegrity an unifying concept of protein folds?

We suggest that the three-dimensional architecture of globular proteins can be described in terms of tensegrets, i.e. structural elements that are held together through attractive and repulsive forces. Hard elements of tensegrets are represented by secondary structure elements, i.e. a-helices and b-strands, while the role of elastic elements is played by attractive and repulsive atomic forces. Characteristics of tensegrets is that they can auto-assemble and that they respond to changes of tension in some part of the entire object through a deformation in another part, thus partially preserving their structure, despite their deformation. This latter property well explains both the folding process and the behavior of globular proteins under mild denaturing conditions, as revealed by the molten globule state.