The Dynamic Transition of Protein Hydration Water

Thin layers of water on biomolecular and other nanostructured surfaces can be supercooled to temperatures not accessible with bulk water. Chen et al. [PNAS 103, 9012 (2006)] suggested that anomalies near 220 K observed by quasi-elastic neutron scattering can be explained by a hidden critical point of bulk water. Based on more sensitive measurements of water on perdeuterated phycocyanin, using the new neutron backscattering spectrometer SPHERES, and an improved data analysis, we present results that show no sign of such a fragile-to-strong transition. The inflection of the elastic intensity at 220 K has a dynamic origin that is compatible with a calorimetric glass transition at 170 K. The temperature dependence of the relaxation times is highly sensitive to data evaluation; it can be brought into perfect agreement with the results of other techniques, without any anomaly.Comment: 4 pages, 3 figures. Phys. Rev. Lett. (in press

The dynamical transition in proteins and non-Gaussian behavior of low frequency modes in Self Consistent Normal Mode Analysis

Self Consistent Normal Mode Analysis (SCNMA) is applied to heme c type cytochrome f to study temperature dependent protein motion. Classical Normal Mode Analysis (NMA) assumes harmonic behavior and the protein Mean Square Displacement (MSD) has a linear dependence on temperature. This is only consistent with low temperature experimental results. To connect the protein vibrational motions between low temperature and physiological temperature, we have incorporated a fitted set of anharmonic potentials into SCNMA. In addition, Quantum Harmonic Oscillator (QHO) theory has been used to calculate the displacement distribution for individual vibrational modes. We find that the modes involving soft bonds exhibit significant non-Gaussian dynamics at physiological temperature, which suggests it may be the cause of the non-Gaussian behavior of the protein motions probed by Elastic Incoherent Neutron Scattering (EINS). The combined theory displays a dynamical transition caused by the softening of few "torsional" modes in the low frequency regime (< 50cm-1or 0.6ps). These modes change from Gaussian to a classical distribution upon heating. Our theory provides an alternative way to understand the microscopic origin of the protein dynamical transition.Comment: 17 pages, 6 figures, 1 tabl

Access Control in a Workstation-Based Distributed Computing Environment

This paper describes the mechanisms employed to control access to system services on the IFS project. We base our distributed computing environment on systems that we trust, and run those systems in physically secure rooms. From that base, we add services, modifying them to interoperate with existing access control mechanisms. Some weaknesses remain in our environment; we conclude with a description of present vulnerabilities and future plans.http://deepblue.lib.umich.edu/bitstream/2027.42/107869/1/citi-tr-90-2.pd

Influence of the Environment Fluctuations on Incoherent Neutron Scattering Functions

In extending the conventional dynamic models, we consider a simple model to account for the environment fluctuations of particle atoms in a protein system and derive the elastic incoherent structure factor (EISF) and the incoherent scattering correlation function C(Q,t) for both the jump dynamics between sites with fluctuating site interspacing and for the diffusion inside a fluctuating sphere. We find that the EISF of the system (or the normalized elastic intensity) is equal to that in the absence of fluctuations averaged over the distribution of site interspacing or sphere radius a. The scattering correlation function is $C(Q,t)=\sum_{n} \psi(t)$, where the average is taken over the Q-dependent effective distribution of relaxation rates \lambda_n(a) and \psi(t) is the correlation function of the length a. When \psi(t)=1, the relaxation of C(Q,t) is exponential for the jump dynamics between sites (since \lambda_n(a) is independent of a) while it is nonexponential for diffusion inside a sphere.Comment: 7 pages, 7 eps figure

High-Pressure Specific-Heat Spectroscopy At The Glass-Transition In O-Terphenyl

Measurements of the enthalpy relaxations in liquid orthoterphenyl in the supercooled state have been carried out using specific-heat spectroscopy over the frequency range from 2 Hz to 6.3 kHz, as a function of temperature and as a function of pressure. The observed α-relaxation peaks in the phase of the complex specific heat show increasing relaxation times τ with increasing pressure at constant temperature, similar to the divergence of τ when the calorimetric glass temperature Tg is approached by lowering the temperature at constant pressure. The temperature and pressure dependence of the measured mean relaxation times τ¯ near Tg are in remarkable agreement with those found by other spectroscopic methods and have been compared with an extended Vogel-Fulcher-Tammann law. However, we find different scaling when the glass transition is approached by cooling or by increasing pressure. This suggests that the assumption of a simple volume-activated process is not adequate

Glass transition in biomolecules and the liquid-liquid critical point of water

Using molecular dynamics simulations, we investigate the relation between the dynamic transitions of biomolecules (lysozyme and DNA) and the dynamic and thermodynamic properties of hydration water. We find that the dynamic transition of the macromolecules, sometimes called a ``protein glass transition'', occurs at the temperature of dynamic crossover in the diffusivity of hydration water, and also coincides with the maxima of the isobaric specific heat $C_P$ and the temperature derivative of the orientational order parameter. We relate these findings to the hypothesis of a liquid-liquid critical point in water. Our simulations are consistent with the possibility that the protein glass transition results from crossing the Widom line, which is defined as the locus of correlation length maxima emanating from the hypothesized second critical point of water.Comment: 10 Pages, 12 figure

A Synthetic Porcine Reproductive and Respiratory Syndrome Virus Strain Confers Unprecedented Levels of Heterologous Protection

Current vaccines do not provide sufficient levels of protection against divergent porcine reproductive and respiratory syndrome virus (PRRSV) strains circulating in the field, mainly due to the substantial variation of the viral genome. We describe here a novel approach to generate a PRRSV vaccine candidate that could confer unprecedented levels of heterologous protection against divergent PRRSV isolates. By using a set of 59 nonredundant, full-genome sequences of type 2 PRRSVs, a consensus genome (designated PRRSV-CON) was generated by aligning these 59 PRRSV full-genome sequences, followed by selecting the most common nucleotide found at each position of the alignment. Next, the synthetic PRRSV-CON strain was generated through the use of reverse genetics. PRRSV-CON replicates as efficiently as our prototype PRRSV strain FL12, both in vitro and in vivo. Importantly, when inoculated into pigs, PRRSV-CON confers significantly broader levels of heterologous protection than does wild-type PRRSV. Collectively, our data demonstrate that PRRSV-CON can serve as an excellent candidate for the development of a broadly protective PRRSV vaccine