Lifetime determination of excited states in106Cd

Two separate experiments using the Differential Decay Curve Method have been performed to extract mean lifetimes of excited states in 106Cd. The medium-spin states of interest were populated by the 98Mo( 12C, 4n) 106Cd reaction performed at the Wright Nuclear Structure Lab., Yale University. From this experiment, two isomeric state mean lifetimes have been deduced. The low-lying states were populated by the 96Mo(13C, 3n)106Cd reaction performed at the Institut für Kernphysik, Universität zu Köln. The mean lifetime of the Iπ = 21 + state was deduced, tentatively, as 16.4(9) ps. This value differs from the previously accepted literature value from Coulomb excitation of 10.43(9) ps.

Local hydrogen reactions of H*2 in a-Si:H

Hydrogen rearrangements at the H*2 complex are used as a model of low energy, local transitions in the two-hydrogen density of states of hydrogenated amorphous silicon (a-Si:H). These are used to account for the low activation energy motion of H observed by nuclear magnetic resonance, the low energy defect annealing of defects formed by bias stress in thin film transistors, and the elimination of hydrogen from the growth zone during the low temperature plasma deposition of a-Si:H. © 1998 Elsevier Science B.V. All rights reserved.

Population of nonnative states of lysozyme variants drives amyloid fibril formation.

The propensity of protein molecules to self-assemble into highly ordered, fibrillar aggregates lies at the heart of understanding many disorders ranging from Alzheimer's disease to systemic lysozyme amyloidosis. In this paper we use highly accurate kinetic measurements of amyloid fibril growth in combination with spectroscopic tools to quantify the effect of modifications in solution conditions and in the amino acid sequence of human lysozyme on its propensity to form amyloid fibrils under acidic conditions. We elucidate and quantify the correlation between the rate of amyloid growth and the population of nonnative states, and we show that changes in amyloidogenicity are almost entirely due to alterations in the stability of the native state, while other regions of the global free-energy surface remain largely unmodified. These results provide insight into the complex dynamics of a macromolecule on a multidimensional energy landscape and point the way for a better understanding of amyloid diseases.