A novel energy landscape model, ELM, for proteins recently explained a collection of incoherent, elastic neutron scattering data from proteins. The ELM of proteins considers the elastic response of the proton and its environment to the energy and momentum exchanged with the neutron. In the ELM, the elastic potential energy is expressed as a sum of a temperature dependent term resulting from equipartition of potential energy among the active degrees of freedom and a wave vector transfer dependent term resulting from the elastic energy stored by the protein during the neutron scattering event. The elastic potential energy involves a new elastobaric coefficient that is proportional to the product of two factors: one factor depends on universal constants and the other on the incident neutron wave vector per degree of freedom. The ELM was tested for dry protein samples with an elastobaric coefficient corresponding to 3 degrees of freedom. A discussion of the data requirements for additional tests of ELM is presented resulting in a call for published data that have not been preprocessed by temperature and wave-vector dependent normalizations.
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