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Register a new userOn the mechanisms responsible of photocurrent in bacteriorhodopsin (Bacteriorhodopsins sense of light)
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Added by
Eleonora Alfinito Dr.
Publication date
2015
fields
Physics
and research's language is
English
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Recently, a growing interest has been addressed to the electrical properties of bacteriorhodopsin (bR), a protein belonging to the transmembrane protein family. To take into account the structure-dependent nature of the current, in a previous set of papers we suggested a mechanism of sequential tunneling among neighbouring amino acids. As a matter of fact, it is well accepted that, when irradiated with green light, bR undergoes a conformational change at a molecular level. Thus, the role played by the protein tertiary-structure in modeling the charge transfer cannot be neglected. The aim of this paper is to go beyond previous models, in the framework of a new branch of electronics, we called proteotronics, which exploits the ability to use proteins as reliable, well understood materials, for the development of novel bioelectronic devices. In particular, the present approach assumes that the conformational change is not the unique transformation that the protein undergoes when irradiated by light. Instead, the light can also promote a free-energy increase of the protein state that, in turn, should modify its internal degree of connectivity, here described by the change in the value of an interaction radius associated with the physical interactions among amino acids. The implemented model enables us to achieve a better agreement between theory and experiments in the region of a low applied bias by preserving the level of agreement at high values of applied bias. Furthermore, results provide new insights on the mechanisms responsible for bR photoresponse.
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In this short note, a correction is made to the recently proposed solution [1] to a 1D biased diffusion model for linear DNA translocation and a new analysis will be given to the data in [1]. It was pointed out [2] by us recently that this 1D linear translocation model is equivalent to the one that was considered by Schrodinger [3] for the Enrenhaft-Millikan measurements [4,5] on electron charge. Here we apply Schrodingers first-passage-time distribution formula to the data set in [1]. It is found that Schrodingers formula can be used to describe the time distribution of DNA translocation in solid-state nanopores. These fittings yield two useful parameters: drift velocity of DNA translocation and diffusion constant of DNA inside the nanopore. The results suggest two regimes of DNA translocation: (I) at low voltages, there are clear deviations from Smoluchowskis linear law of electrophoresis [6] which we attribute to the entropic barrier effects; (II) at high voltages, the translocation velocity is a linear function of the applied electric field. In regime II, the apparent diffusion constant exhibits a quadratic dependence on applied electric field, suggesting a mechanism of Taylor dispersion effect likely due the electro-osmotic flow field in the nanopore channel. This analysis yields a dispersion-free diffusion constant value for the segment of DNA inside the nanopore which is in agreement with Stokes-Einstein theory quantitatively. The implication of Schrodingers formula for DNA sequencing is discussed.
We report a theoretical study of DNA flexibility and quantitatively predict the ring closure probability as a function of DNA contour length. Recent experimental studies show that the flexibility of short DNA fragments (as compared to the persistence length of DNA l_P~150 base pairs) cannot be described by the traditional worm-like chain (WLC) model, e.g., the observed ring closure probability is much higher than predicted. To explain these observations, DNA flexibility is investigated with explicit considerations of a new length scale l_D~10 base pairs, over which DNA local bend angles are correlated. In this correlated worm-like chain (C-WLC) model, a finite length correction term is analytically derived and the persistence length is found to be contour length dependent. While our model reduces to the traditional worm-like chain model when treating long DNA at length scales much larger than l_P, it predicts that DNA becomes much more flexible at shorter sizes, which helps explain recent cyclization measurements of short DNA fragments around 100 base pairs.
A theoretical analysis of the unfolding pathway of simple modular proteins in length- controlled pulling experiments is put forward. Within this framework, we predict the first module to unfold in a chain of identical units, emphasizing the ranges of pulling speeds in which we expect our theory to hold. These theoretical predictions are checked by means of steered molecular dynamics of a simple construct, specifically a chain composed of two coiled-coils motives, where anisotropic features are revealed. These simulations also allow us to give an estimate for the range of pulling velocities in which our theoretical approach is valid.
Single molecule force spectroscopy of DNA strands adsorbed at surfaces is a powerful technique used in air or liquid environments to quantify their mechanical properties. Although the force responses are limited to unfolding events so far, single base detection might be possible in more drastic cleanliness conditions such as ultra high vacuum. Here, we report on high resolution imaging and pulling attempts at low temperature (5K) of a single strand DNA (ssDNA) molecules composed of 20 cytosine bases adsorbed on Au(111) by scanning probe microscopy and numerical calculations. Using electrospray deposition technique, the ssDNA were successfully transferred from solution onto a surface kept in ultra high vacuum. Real space characterizations reveal that the ssDNA have an amorphous structure on gold in agreement with numerical calculations. Subsequent substrate annealing promotes the desorption of solvent molecules, DNA as individual molecules as well as the formation of DNA self assemblies. Furthermore, pulling experiments by force spectroscopy have been conducted to measure the mechanical response of the ssDNA while detaching. A periodic pattern of 0.2 to 0.3nm is observed in the force curve which arises from the stick slip of single nucleotide bases over the gold. Although an intra molecular response is obtained in the force curve, a clear distinction of each nucleotide detachment is not possible due the complex structure of ssDNA adsorbed on gold.
We present a computational study on the folding and aggregation of proteins in aqueous environment, as function of its concentration. We show how the increase of the concentration of individual protein species can induce a partial unfolding of the native conformation without the occurrence of aggregates. A further increment of the protein concentration results in the complete loss of the folded structures and induces the formation of protein aggregates. We discuss the effect of the protein interface on the water fluctuations in the protein hydration shell and their relevance in the protein-protein interaction.
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