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H-bonds are known to play an important role in the folding of proteins intothree-dimensional structures, which in turn determine their diverse functions.The conformations around H-bonds are important, in that they can be non-localalong the backbone and are therefore not captured by the methods such asRamachandran plots. We study the relationship between the geometry of H-bondsin proteins, expressed as a spatial rotation between the two bonded peptideunits, and their topology, expressed as a subgraph of the protein fatgraph. Wedescribe two experiments to predict H-bond rotations from their correspondingsubgraphs. The first method is based on sequence alignment between sequences ofthe signed lengths of H-bonds measured along the backbone. The second method isbased on finding an exact match between the descriptions of subgraphs aroundH-bonds. We find that 88.14% of the predictions lie inside the ball, centredaround the true rotation, occupying just 1% of the volume of the rotation spaceSO(3).

Prediction of H-Bond Rotations from Protein H-Bond Topology