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. Author manuscript; available in PMC: 2014 Jan 1.
Published in final edited form as: Proteins. 2012 Sep 18;81(1):18–39. doi: 10.1002/prot.24150

Table II.

Types of perturbations

Type Parameter Continuous Residues affected Where usually found
Shear* Primary shear angle Yes 4 Helices
Backrub Primary backrub angle Yes 3 β sheets, loops
Loop closure adjustment* Solution from discrete set No 3 Loops
Secondary structure adjustment* Solution from discrete set No 3–4 Loop-helix or loop-sheet borders
Partial structure switch Structure from discrete set No As desired Anywhere
Full structure switch Structure from discrete set No All Entire protein
Proline flip Boolean: flip or no flip No 1 Prolines
*

These perturbations cannot, to our knowledge, be performed by any previous protein design algorithm. DEEPer also offers novel combinations of perturbations that have been modeled previously; for example, no previous provable algorithm modeled overlapping backrubs. DEEPer is also novel in combining these perturbations with continuous sidechain flexibility, which is represented as orthogonal to perturbations in conformational space.