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1.
Phys Rev Lett ; 111(15): 157201, 2013 Oct 11.
Article in English | MEDLINE | ID: mdl-24160622

ABSTRACT

We study the spin-1/2 quantum Heisenberg antiferromagnet on a Bethe lattice diluted to the percolation threshold. Dilution creates areas of even or odd sublattice imbalance resulting in "dangling spins" [L. Wang and A. W. Sandvik, Phys. Rev. Lett. 97, 117204 (2006); Phys. Rev. B 81, 054417 (2010)]. These collectively act as "emergent" spin-1/2 degrees of freedom and are responsible for the creation of a set of low-lying "quasidegenerate states." Using density matrix renormalization group calculations, we detect the presence and location of these emergent spins. We find an effective Hamiltonian of these emergent spins, with Heisenberg interactions that decay exponentially with the distance between them.

2.
Phys Biol ; 4(4): 344-54, 2008 Jan 08.
Article in English | MEDLINE | ID: mdl-18185012

ABSTRACT

Ligand binding to receptors is the initial event in many signaling processes, and a quantitative understanding of this interaction is important for modeling cell behavior. In this paper, we study the kinetics of reversible ligand binding to receptors on a spherical cell surface using a self-consistent stochastic theory. Binding, dissociation, diffusion and rebinding of ligands are incorporated into the theory in a systematic manner. We derive explicitly the time evolution of the ligand-bound receptor fraction p(t) in various regimes. Contrary to the commonly accepted view, we find that the well-known Berg-Purcell scaling for the association rate is modified as a function of time. Specifically, the effective on-rate changes non-monotonically as a function of time and equals the intrinsic rate at very early as well as late times, while being approximately equal to the Berg-Purcell value at intermediate times. The effective dissociation rate, as it appears in the binding curve or measured in a dissociation experiment, is strongly modified by rebinding events and assumes the Berg-Purcell value except at very late times, where the decay is algebraic and not exponential. In equilibrium, the ligand concentration everywhere in the solution is the same and equals its spatial mean, thus ensuring that there is no depletion in the vicinity of the cell. Implications of our results for binding experiments and numerical simulations of ligand-receptor systems are also discussed.


Subject(s)
Biophysics/methods , Cell Physiological Phenomena , Ligands , Animals , Cell Membrane , Chemotaxis , Computer Simulation , Diffusion , Escherichia coli/metabolism , Humans , Kinetics , Models, Biological , Models, Statistical , Protein Binding , Time Factors
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