AI Article Synopsis
- The paper explores how anisotropic atomic movements in proteins affect incoherent neutron scattering intensities derived from powder samples.
- It uses multipole series to represent correlation functions, with each term reflecting varying levels of intrinsic motional anisotropy.
- The findings, illustrated through an analytical model and simulations of lysozyme, demonstrate that the anisotropic motion of protein atoms significantly influences the scattering intensity.
Article Abstract
This paper addresses the question to which extent anisotropic atomic motions in proteins impact angular-averaged incoherent neutron scattering intensities, which are typically recorded for powder samples. For this purpose, the relevant correlation functions are represented as multipole series in which each term corresponds to a different degree of intrinsic motional anisotropy. The approach is illustrated by a simple analytical model and by a simulation-based example for lysozyme, considering in both cases the elastic incoherent structure factor. The second example shows that the motional anisotropy of the protein atoms is considerable and contributes significantly to the scattering intensity.
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| http://dx.doi.org/10.1063/1.4769782 | DOI Listing |
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