3,065 research outputs found
Cooperative Origin of Low-Density Domains in Liquid Water
We study the size of clusters formed by water molecules possessing large
enough tetrahedrality with respect to their nearest neighbors. Using Monte
Carlo simulation of the SPC/E model of water, together with a geometric
analysis based on Voronoi tessellation, we find that regions of lower density
than the bulk are formed by accretion of molecules into clusters exceeding a
minimum size. Clusters are predominantly linear objects and become less compact
as they grow until they reach a size beyond which further accretion is not
accompanied by a density decrease. The results suggest that the formation of
"ice-like" regions in liquid water is cooperative.Comment: 16 pages, 6 figure
Physics of the liquid-liquid critical point
Within the inherent structure (IS) thermodynamic formalism introduced by
Stillinger and Weber [F. H. Stillinger and T. A. Weber, Phys. Rev. A {\bf 25},
978 (1982)] we address the basic question of the physics of the liquid-liquid
transition and of density maxima observed in some complex liquids such as water
by identifying, for the first time, the statistical properties of the potential
energy landscape (PEL) responsible for these anomalies.
We also provide evidence of the connection between density anomalies and the
liquid-liquid critical point. Within the simple (and physically transparent)
model discussed, density anomalies do imply the existence of a liquid-liquid
transition.Comment: Physical Review Letters, in publicatio
High frequency longitudinal and transverse dynamics in water
High-resolution, inelastic x-ray scattering measurements of the dynamic
structure factor S(Q,\omega) of liquid water have been performed for wave
vectors Q between 4 and 30 nm^-1 in distinctly different thermodynamic
conditions (T= 263 - 420 K ; at, or close to, ambient pressure and at P = 2
kbar). In agreement with previous inelastic x-ray and neutron studies, the
presence of two inelastic contributions (one dispersing with Q and the other
almost non-dispersive) is confirmed. The study of their temperature- and
Q-dependence provides strong support for a dynamics of liquid water controlled
by the structural relaxation process. A viscoelastic analysis of the
Q-dispersing mode, associated with the longitudinal dynamics, reveals that the
sound velocity undergoes the complete transition from the adiabatic sound
velocity (c_0) (viscous limit) to the infinite frequency sound velocity
(c_\infinity) (elastic limit). On decreasing Q, as the transition regime is
approached from the elastic side, we observe a decrease of the intensity of the
second, weakly dispersing feature, which completely disappears when the viscous
regime is reached. These findings unambiguously identify the second excitation
to be a signature of the transverse dynamics with a longitudinal symmetry
component, which becomes visible in the S(Q,\omega) as soon as the purely
viscous regime is left.Comment: 28 pages, 12 figure
Adsorption-desorption kinetics in nanoscopically confined oligomer films under shear
The method of molecular dynamics computer simulations is employed to study oligomer melts confined in ultra-thin films and subjected to shear. The focus is on the self-diffusion of oligomers near attractive surfaces and on their desorption, together with the effects of increasing energy of adsorption and shear. It is found that the mobility of the oligomers near an attractive surface is strongly decreased. Moreover, although shearing the system forces the chains to stretch parallel to the surfaces and thus increase the energy of adsorption per chain, flow also promotes desorption. The study of chain desorption kinetics reveals the molecular processes responsible for the enhancement of desorption under shear. They involve sequences of conformations starting with a desorbed tail and proceeding in a very fast, correlated, segment-by-segment manner to the desorption of the oligomers from the surfaces.
Supercooled confined water and the Mode Coupling crossover temperature
We present a Molecular Dynamics study of the single particle dynamics of
supercooled water confined in a silica pore. Two dynamical regimes are found:
close to the hydrophilic substrate molecules are below the Mode Coupling
crossover temperature, , already at ambient temperature. The water closer
to the center of the pore (free water) approaches upon supercooling as
predicted by Mode Coupling Theories. For free water the crossover temperature
and crossover exponent are extracted from power-law fits to both the
diffusion coefficient and the relaxation time of the late region.Comment: To be published, Phys. Rev. Lett., 4 pages, 3 figures, revTeX, minor
changes in the figures, references added, changes in the tex
Origin of entropy convergence in hydrophobic hydration and protein folding
An information theory model is used to construct a molecular explanation why
hydrophobic solvation entropies measured in calorimetry of protein unfolding
converge at a common temperature. The entropy convergence follows from the weak
temperature dependence of occupancy fluctuations for molecular-scale volumes in
water. The macroscopic expression of the contrasting entropic behavior between
water and common organic solvents is the relative temperature insensitivity of
the water isothermal compressibility. The information theory model provides a
quantitative description of small molecule hydration and predicts a negative
entropy at convergence. Interpretations of entropic contributions to protein
folding should account for this result.Comment: Phys. Rev. Letts. (in press 1996), 3 pages, 3 figure
Molecular dynamics simulation of polymer helix formation using rigid-link methods
Molecular dynamics simulations are used to study structure formation in
simple model polymer chains that are subject to excluded volume and torsional
interactions. The changing conformations exhibited by chains of different
lengths under gradual cooling are followed until each reaches a state from
which no further change is possible. The interactions are chosen so that the
true ground state is a helix, and a high proportion of simulation runs succeed
in reaching this state; the fraction that manage to form defect-free helices is
a function of both chain length and cooling rate. In order to demonstrate
behavior analogous to the formation of protein tertiary structure, additional
attractive interactions are introduced into the model, leading to the
appearance of aligned, antiparallel helix pairs. The simulations employ a
computational approach that deals directly with the internal coordinates in a
recursive manner; this representation is able to maintain constant bond lengths
and angles without the necessity of treating them as an algebraic constraint
problem supplementary to the equations of motion.Comment: 15 pages, 14 figure
Secondary-Structure Design of Proteins by a Backbone Torsion Energy
We propose a new backbone-torsion-energy term in the force field for protein
systems. This torsion-energy term is represented by a double Fourier series in
two variables, the backbone dihedral angles phi and psi. It gives a natural
representation of the torsion energy in the Ramachandran space in the sense
that any two-dimensional energy surface periodic in both phi and psi can be
expanded by the double Fourier series. We can then easily control
secondary-structure-forming tendencies by modifying the torsion-energy surface.
For instance, we can increase/decrease the alpha-helix-forming-tendencies by
lowering/raising the torsion-energy surface in the alpha-helix region and
likewise increase/decrease the beta-sheet-forming tendencies by
lowering/raising the surface in the beta-sheet region in the Ramachandran
space. We applied our approach to AMBER parm94 and AMBER parm96 force fields
and demonstrated that our modifications of the torsion-energy terms resulted in
the expected changes of secondary-structure-forming-tendencies by performing
folding simulations of alpha-helical and beta-hairpin peptides.Comment: 13 pages, (Revtex4), 5 figure
Hydrogen Bond Dynamics Near A Micellar Surface: Origin of the Universal Slow Relaxation at Complex Aqueous Interfaces
The dynamics of hydrogen bonds among water molecules themselves and with the
polar head groups (PHG) at a micellar surface have been investigated by long
molecular dynamics simulations. The lifetime of the hydrogen bond between a PHG
and a water molecule is found to be much longer than that between any two water
molecules, and is likely to be a general feature of hydrophilic surfaces of
organized assemblies. Analyses of individual water trajectories suggest that
water molecules can remain bound to the micellar surface for more than a
hundred picosecond. The activation energy for such a transition from the bound
to a free state for the water molecules is estimated to be about 3.5kcal/mole.Comment: 12 pages. Phys. Rev. Lett. (Accepted) (2002
Multi-Scale Simulations Provide Supporting Evidence for the Hypothesis of Intramolecular Protein Translocation in GroEL/GroES Complexes
The biological function of chaperone complexes is to assist the folding of non-native proteins. The widely studied GroEL chaperonin is a double-barreled complex that can trap non-native proteins in one of its two barrels. The ATP-driven binding of a GroES cap then results in a major structural change of the chamber where the substrate is trapped and initiates a refolding attempt. The two barrels operate anti-synchronously. The central region between the two barrels contains a high concentration of disordered protein chains, the role of which was thus far unclear. In this work we report a combination of atomistic and coarse-grained simulations that probe the structure and dynamics of the equatorial region of the GroEL/GroES chaperonin complex. Surprisingly, our simulations show that the equatorial region provides a translocation channel that will block the passage of folded proteins but allows the passage of secondary units with the diameter of an alpha-helix. We compute the free-energy barrier that has to be overcome during translocation and find that it can easily be crossed under the influence of thermal fluctuations. Hence, strongly non-native proteins can be squeezed like toothpaste from one barrel to the next where they will refold. Proteins that are already fairly close to the native state will not translocate but can refold in the chamber where they were trapped. Several experimental results are compatible with this scenario, and in the case of the experiments of Martin and Hartl, intra chaperonin translocation could explain why under physiological crowding conditions the chaperonin does not release the substrate protein
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