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Journal of Structural Biology, Vol.125, No.1, 1-10, 1999
Side-chains configurations in coiled coils revealed by the 5.15-angstrom meridional reflection on hard alpha-keratin X-ray diffraction patterns
The origin of the 5.15-Angstrom meridional reflection on hard alpha-keratin X-ray diffraction patterns is discussed in terms of side-chains conformations. We show it to reveal specific configurations of the side chains which are common to all two-stranded alpha-helical coiled coils. Combining literature data on crystallised coiled coil pieces and molecular dynamics results with our X-ray diffraction pattern simulations, we propose rules for the attribution of chi(1) torsion angles for coiled coils involved in fibres whose structure cannot be resolved at atomic resolution: in a (a b c d e f g) heptad repeat, a and d residues, respectively, adopt mean t and g(+) configurations, whereas statistical rules are given for the other residues.