RSMR experiments with57Fe radiation were performed on myoglobin. An areasensitive detector was employed for simultaneous angular dependent collection of the scattered quanta up to a maximum angle 2θ of 17‡. Experimental data of polycrystalline and lyophilized myoglobin are compared with computer calculations of the scattering which are based on the atomic coordinates determined by X-ray structure analysis. Special attention has been paid to the influence of coherence effects from collectively moving parts of the protein. A simple model is introduced in order to take into account these segmental motions. Our first results indicate that the sizes of collectively moving segments are comparable with spheres of about 6 å in diameter in dry myoglobin. In myoglobin crystals, where the molecules are surrounded by large hydration shells, the movements appear to be correlated in segments with sizes comparable to helices.
The distorted wave is introduced into the relativistic impulse approximation to generate the Dirac optical potentials for proton elastic scattering. Those potentials, produced by folding the target ground state wavefunction with the free nucleon-nucleon interactions, are used to reevaluate scattering observables, such as differential cross section, analysing power and spin rotation function, for proton elastic scattering from ^12C and ^16O at Elab = 200 MeV, respectively. The inclusion of the distorted wave in the original relativistic impulse approximation has brought out better results of the observables, especially at small scattering angles. 相似文献