Morphs: Difference between revisions

Many proteins perform their functions without major conformational changes. In contract, some proteins must undergo major changes in secondary, tertiary, or quaternary structure in order to perform their functions. In quite a few cases, investigators have succeeded in obtaining empirically determined structures for a protein in two or more conformations. The challenge for visualization is then to be able to follow the movements of each portion between the two conformations. When the differences are small, simply toggling an image between the two states is adequate. David Richardson's MAGE (1992) is supported supports visual toggling between macromolecular conformations, and hundreds of kinemages take advantage of this capability. Here is an example from hemoglobin. However, when some of the conformational differences are large, toggling is not sufficient to allow one to follow the transition made by each portion as the image jumps between the two conformations. The purpose of morphing is to smooth the visual transition, making it easier to see the structural relationships between the two empirical conformations.