QUASIELASTIC NEUTRON SCATTERING PROBES PROTEIN DYNAMICS.
To understand the changes in protein dynamics that occur in the final stages of folding, scientists at NIST have used quasielastic neutron scattering to probe the differences in the dynamics between the native state and the almost completely folded, molten globule state of the protein bovine a-lactalbumin. The results, show that the side-chain protons in the molten globules are significantly more mobile than those in the native protein. Moreover, the length scale of the motion, information that is uniquely provided by neutron, spectroscopic techniques, is substantially longer in the molten globule state compared to that in the more compact native state.
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|Publication:||Journal of Research of the National Institute of Standards and Technology|
|Article Type:||Brief Article|
|Date:||Nov 1, 2000|
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