Neutron Compton scattering from selectively deuterated acetanilide

With the aim of developing the application of neutron Compton scattering (NCS) to molecular systems of biophysical interest, we are using the Compton spectrometer EVS at ISIS to characterize the momentum distribution of protons in peptide groups. In this contribution we present NCS measurements of the recoil peak (Compton profile) due to the amide proton in otherwise fully deuterated acetanilide (ACN), a widely studied model system for H-bonding and energy transfer in biomolecules. We obtain values for the average width of the potential well of the amide proton and its mean kinetic energy. Deviations from the Gaussian form of the Compton profile, analyzed on the basis of an expansion due to Sears, provide data relating to the Laplacian of the proton potential. (C) 1998 Elsevier Science B.V. All rights reserved

Proton mobilities in crambin and glutathione-S-transferase

Let (M,F) be a compact codimension-one foliated manifold whose leaves are equipped with Riemannian metrics, and consider continuous functions on M that are harmonic along the leaves of F. If every such function is constant on leaves we say that (M,F) has the Liouville property. Our main result is that codimension-one foliated bundles over compact negatively curved manifolds satisfy the Liouville property. Related results for R-covered foliations, as well as for discrete group actions and discrete harmonic functions, are also established

Anharmonic Behavior in the Multisubunit Protein Apoferritin as Revealed by Quasi-Elastic Neuton Scattering

Quasi-elastic neutron scattering (QENS) has been used to study the deviation from Debye-law harmonic behavior in lyophilized and hydrated apoferritin, a naturally occurring, multisubunit protein. Whereas analysis of the measured mean squared displacement (msd) parameter reveals a hydration-dependent inflection above 240 K, characteristic of diffusive motion, a hydration-independent inflection is observed at 100 K. The mechanism responsible for this low-temperature anharmonic response is further investigated, via analysis of the elastic incoherent neutron scattering intensity, by applying models developed to describe side-group motion in glassy polymers. Our results suggest that the deviation from harmonic behavior is due to the onset of methyl group rotations which exhibit a broad distribution of activated processes (Ea,ave ) 12.2 kJ · mol-1, σ ) 5.0 kJ · mol-1). Our results are likened to those reported for other proteins

Probing the Structure and Dynamics of Cells, Cell Components and Endogenous Nanoparticles Under Extreme Conditions with Neutrons

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