Determination of locked interfaces in biomolecular complexes using Haptimol_RD

Georgios Iakovou, Stephen Laycock, Steven Hayward

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


Interactive haptics-assisted docking provides a virtual environment for the study of molecular complex formation. It enables the user to interact with the virtual molecules, experience the interaction forces via their sense of touch, and gain insights about the docking process itself. Here we use a recently developed haptics software tool, Haptimol_RD, for the rigid docking of protein subunits to form complexes. Dimers, both homo and hetero, are loaded into the software with their subunits separated in space for the purpose of assessing whether they can be brought back into the correct docking pose via rigid-body movements. Four dimers were classified into two types: two with an interwinding subunit interface and two with a non-interwinding subunit interface. It was found that the two with an interwinding interface could not be docked whereas the two with the non-interwinding interface could be. For the two that could be docked a “sucking” effect could be felt on the haptic device when the correct binding pose was approached which is associated with a minimum in the interaction energy. It is clear that for those that could not be docked, the conformation of one or both of the subunits must change upon docking. This leads to the steric-based concept of a locked or non-locked interface. Non-locked interfaces have shapes that allow the subunits to come together or come apart without the necessity of intra-subunit conformational change, whereas locked interfaces require a conformational change within one or both subunits for them to be able to come apart.
Original languageEnglish
Pages (from-to)97-103
Number of pages7
JournalBiophysics and Physicobiology
Publication statusPublished - 14 Jul 2016


  • protein-protein interaction
  • Haptic Feedback
  • Force Feedback
  • Protein Docking
  • interwinding interface

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