اشترك بالحزمة الذهبية واحصل على وصول غير محدود شمرا أكاديميا
تسجيل مستخدم جديدHow proteins squeeze through polymer networks: a Cartesian lattice study
159
0
0.0
(
0
)
اسأل ChatGPT حول البحث
ﻻ يوجد ملخص باللغة العربية
In this paper a lattice model for the diffusional transport of particles in the interphase cell nucleus is proposed. The dynamic behaviour of single chains on the lattice is investigated and Rouse scaling is verified. Dynamical dense networks are created by a combined version of the bond fluctuation method and a Metropolis Monte Carlo algorithm. Semidilute behaviour of the dense chain networks is shown. By comparing diffusion of particles in a static and a dynamical chain network, we demonstrate that chain diffusion does not alter the diffusion process of small particles. However, we prove that a dynamical network facilitates the transport of large particles. By weighting the mean square displacement trajectories of particles in the static chain network data from the dynamical network can be reconstructed. Additionally, it is shown that subdiffusive behaviour of particles on short time scales results from trapping processes in the crowded environment of the chain network. In the presented model a protein with 30 nm diameter has an effective diffusion coefficient of 1.24E-11 m^2/s in a chromatin fiber network.
قيم البحث
اقرأ أيضاً
The diffusion-controlled limit of reaction times for site-specific DNA-binding proteins is derived from first principles. We follow the generally accepted concept that a protein propagates via two competitive modes, a three-dimensional diffusion in s
pace and a one-dimensional sliding along the DNA. However, our theoretical treatment of the problem is new. The accuracy of our analytical model is verified by numerical simulations. The results confirm that the unspecific binding of protein to DNA, combined with sliding, is capable to reduce the reaction times significantly.
This paper reports all-atom computer simulations of five phospholipid membranes (DMPC, DPPC, DMPG, DMPS, and DMPSH) with focus on the thermal equilibrium fluctuations of volume, energy, area, thickness, and chain order. At constant temperature and pr
essure, volume and energy exhibit strong correlations of their slow fluctuations (defined by averaging over 0.5 nanosecond). These quantities, on the other hand, do not correlate significantly with area, thickness, or chain order. The correlations are mainly reported for the fluid phase, but we also give some results for the ordered (gel) phase of two membranes, showing a similar picture. The cause of the observed strong correlations is identified by splitting volume and energy into contributions from tails, heads, and water, and showing that the slow volume-energy fluctuations derive from van der Waals interactions of the tail region; they are thus analogous to the similar strong correlations recently observed in computer simulations of the Lennard-Jones and other simple van der Waals type liquids [U. R. Pedersen et al., Phys. Rev. Lett. 2008, 100, 015701]. The strong correlations reported here confirm one crucial assumption of a recent theory for nerve signal propagation proposed by Heimburg and Jackson [T. Heimburg and A. D. Jackson, Proc. Natl. Acad. Sci. 2005, 102, 9790-9795].
Realistic 3D-conformations of protein structures can be embedded in a cubic lattice using exclusively integer numbers, additions, subtractions and boolean operations.
Magnetic resonance imaging (MRI) is a non-invasive and label-free technique widely used in medical diagnosis and life science research, and its success has benefited greatly from continuing efforts on enhancing contrast and resolution. Here we report
ed nanoscale MRI in a single cell using an atomic-size quantum sensor. With nitrogen-vacancy center in diamond, the intracellular protein ferritin has been imaged with a spatial resolution of ~ 10 nanometers, and ferritin-containing organelles were co-localized by correlative MRI and electron microscopy. Comparing to the current micrometer resolution in current state-of-art conventional MRI, our approach represents a 100-fold enhancement, and paves the way for MRI of intracellular proteins.
Within the cell, biopolymers are often situated in constrained, fluid environments, e.g., cytoskeletal networks, stretched DNAs in chromatin. It is of paramount importance to understand quantitatively how they, utilizing their flexibility, optimally
respond to a minute signal, which is, in general, temporally fluctuating far away from equilibrium. To this end, we analytically study viscoelastic response and associated stochastic resonance in a stretched single semi-flexible chain to an oscillatory force or electric field. Including hydrodynamic interactions between chain segments, we evaluate dynamics of the polymer extension in coherent response to the force or field. We find power amplification factor of the response at a noise-strength (temperature) can attain the maximum that grows as the chain length increases, indicative of an entropic stochastic resonance (ESR). In particular for a charged chain under an electric field, we find that the maximum also occurs at an optimal chain length, a new feature of ESR. The hydrodynamic interaction is found to enhance the power amplification, representing unique polymer cooperativity which the fluid background imparts despite its overdamping nature. For the slow oscillatory force, the resonance behavior is explained by the chain undulation of the longest wavelength. This novel ESR phenomenon suggests how a biopolymer self-organizes in an overdamping environment, utilizing its flexibility and thermal fluctuations.
سجل دخول لتتمكن من نشر تعليقات
التعليقات
جاري جلب التعليقات
سجل دخول لتتمكن من متابعة معايير البحث التي قمت باختيارها
