Abstract
Analysis of 13 high-resolution protein X-ray crystal structures shows that 1204 (24%) of all the 4974 hydrogen bonds are of the bifurcated three-center type with the donor X-H opposing two acceptors A1, A2. They occur systematically in α-helices where 90% of the hydrogen bonds are of this type; the major component is (n+4)N-H…O=C(n) as expected for a 3.613 α-helix, and the minor component is (n+4)N-H…O=C(n+1), as observed in 310 helices; distortions at the C-temini of α-helices are stabilized by three-center bonds, In β-sheets 40% of the hydrogen bonds are three-centered. The frequent occurrence of three-center hydrogen bonds suggests that they should not be neglected in protein structural studies.
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