The dynamics of Ribonuclease A was explored in the full range of time and length-scales accessible by neutron spectroscopy, on timeof- flight, backscattering and spin-echo spectrometers. Samples were examined in dry and hydrated powder forms and in concentrated and dilute solutions. The aim of the study was an experimental characterisation of the full variety of protein dynamics arising from stabilisation forces. The results provide a benchmark against which other sample dynamics can be compared.
A benchmark for protein dynamics: Ribonuclease A measured by neutron scattering in a large wavevector-energy transfer range
Francesca Natali;Andrea Orecchini;
2008
Abstract
The dynamics of Ribonuclease A was explored in the full range of time and length-scales accessible by neutron spectroscopy, on timeof- flight, backscattering and spin-echo spectrometers. Samples were examined in dry and hydrated powder forms and in concentrated and dilute solutions. The aim of the study was an experimental characterisation of the full variety of protein dynamics arising from stabilisation forces. The results provide a benchmark against which other sample dynamics can be compared.File in questo prodotto:
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