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 alpha-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 3.6(13) alpha-helix, and the minor component is (n + 4)N-H ... O = C(n + 1), as observed in 3(10) helices; distortions at the C-termini of alpha-helices are stabilized by three-center bonds. In beta-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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Preissner R,Egner U,Saenger Wdoi
10.1016/0014-5793(91)81032-4subject
Has Abstractpub_date
1991-08-19 00:00:00pages
192-6issue
1-2eissn
0014-5793issn
1873-3468journal_volume
288pub_type
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