Related papers: Modulators Selectively Reshape alpha-Synuclein Pha…
The phase behavior of charged rods in the presence of inter-rod linkers is studied theoretically as a model for the equilibrium behavior underlying the organization of actin filaments by linker proteins in the cytoskeleton. The presence of…
The existence, stability and movability of breathers in a model for alpha-helix proteins is studied. This model basically consists a chain of dipole moments parallel to it. The existence of localized linear modes brings about that the…
Electric fields are increasingly used for coherently manipulating spin states in semiconductor and molecular systems. Here we discuss the spin manipulation allowed by the modulation of the main parameters entering the Hamiltonians of…
The temporal and spatial development of Parkinson's disease has been characterised as the progressive formation of {\alpha}-synuclein aggregations through susceptible neuronal pathways. This article describes a new model for this…
Protein folding, peptide aggregation and crystallization, as well as adsorption of molecules on soft or solid substrates have an essential feature in common: In all these processes, structure formation is guided by a collective, cooperative…
Neuromodulatory receptors in presynaptic position have the ability to suppress synaptic transmission for seconds to minutes when fully engaged. This effectively alters the synaptic strength of a connection. Much work on neuromodulation has…
Parkinsons disease (PD) alters cortical neural dynamics, yet reliable non-invasive electrophysiological biomarkers remain elusive. This study examined whether interpretable EEG features capturing complementary aspects of neural dynamics can…
We study a minimal extension of the worm-like chain to describe polypeptides having alpha-helical secondary structure. In this model presence/absence of secondary structure enters as a scalar variable that controls the local chain bending…
While all the information required for the folding of a protein is contained in its amino acid sequence, one has not yet learned how to extract this information to predict the three--dimensional, biologically active, native conformation of…
Mutations in proteins can have deleterious effects on a protein's stability and function, which ultimately causes particular diseases. Genetically inherited muscular dystrophies (MDs) include several genetic diseases, which cause increasing…
We study numerically the interplay of disorder and attractive interactions for spin-1/2 fermions in the three-dimensional Hubbard model. The results obtained by projector quantum Monte Carlo simulations show that at moderate disorder,…
The intrinsic property of proteins to form structural motifs such as alpha-helices and beta-sheets leads to a complex phase behavior in which proteins can assemble into various types of aggregates including crystals, liquidlike phases of…
Globular proteins are expected to assume folds with fixed secondary structures, alpha-helices and beta-sheets. Fold-switching proteins challenge this expectation by remodeling their secondary and/or tertiary structures in response to…
Phase transitions induced by varying the strength of disorder in the large-q state Potts model in 3d are studied by analytical and numerical methods. By switching on the disorder the transition stays of first order, but different…
Two-dimensional shape-morphing networks are common in biological systems and have garnered attention due to their nontrivial physical properties that emanate from their cellular nature. Here, we present the fabrication and characterization…
We carried out dynamic force manipulations $in$ $silico$ on a variety of superhelical protein fragments from myosin, chemotaxis receptor, vimentin, fibrin, and phenylalanine zippers that vary in size and topology of their $\alpha$-helical…
If a binary liquid mixture, composed of two alternative species with equal amounts, is quenched from a high temperature to a low temperature, below the critical point of demixing, then the mixture will phase separate through a process known…
The folding dynamics of small single-domain proteins is a current focus of simulations and experiments. Many of these proteins are 'two-state folders', i.e. proteins that fold rather directly from the denatured state to the native state,…
We investigate the phase transition properties of the polymer-Potts model, a chain composed of monomers with magnetic degrees of freedom, with the motivation to study the conformation and mark switching dynamics of chromatin. By the…
Experimental evidence suggests that the folding and aggregation of the amyloid $\beta$-protein (A$\beta$) into oligomers is a key pathogenetic event in Alzheimer's disease (AD). Inhibiting the pathologic folding and oligomerization of…