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1.
Phys Chem Chem Phys ; 16(29): 15597-607, 2014 Aug 07.
Article in English | MEDLINE | ID: mdl-24955728

ABSTRACT

Hematite (α-Fe2O3) nanoparticles of two different shapes but of same size (ca. 40 nm) were dispersed in PEDOT:PSS matrices in various concentration ranges (0-7 wt%) to study the consequent changes in conductivity in the dark and under solar illumination conditions. Within a distinct range of concentration, a distinct increase in the conductivity was observed for both spherical and cubical particle population. We ascribed this effect to the generalized Poole-Frenkel theory of conduction in conjunction with the basic depletion width properties of heterojunctions and electrostatic dipole moments, and verified our assumptions through data fitting. A difference in conductivity between sphere- and cube-based α-Fe2O3-PEDOT:PSS nanocomposites was also observed and ascribed to the electrostatic edge effect on the nanoparticles. The dispersion of α-Fe2O3 nanocrystals was confirmed by high-resolution electron microscopy, whereas the electrical properties and modulations thereof were followed by recording current-voltage characteristics.

2.
Phys Rev E Stat Nonlin Soft Matter Phys ; 77(2 Pt 1): 021910, 2008 Feb.
Article in English | MEDLINE | ID: mdl-18352054

ABSTRACT

In order to investigate the protein folding-unfolding process, dynamic light scattering (DLS) and atomic force microscopy (AFM) imaging were used to study two fragments of the muscle cardiac protein beta-connectin, also known as titin. Both fragments belong to the I band of the sarcomer, and they are composed of four domains from I(27) to I(30) (tetramer) and eight domains from I(27) to I(34) (octamer). DLS measurements provide the size of both fragments as a function of temperature from 20 up to 86 degrees C, and show a thermal denaturation due to temperature increase. AFM imaging of both fragments in the native state reveals a homogeneous and uniform distribution of comparable structures. The DLS and AFM techniques turn out to be complementary for size measurements of the fragments and fragment aggregates. An unexpected result is that the octamer folds into a smaller structure than the tetramer and the unfolded octamer is also smaller than the unfolded tetramer. This feature seems related to the significance of the hydrophobic interactions between domains of the fragment. The longer the fragment, the more easily the hydrophobic parts of the domains interact with each other. The fragment aggregation behavior, in particular conditions, is also revealed by both DLS and AFM as a process that is parallel to the folding-unfolding transition.


Subject(s)
Models, Chemical , Models, Molecular , Muscle Proteins/chemistry , Muscle Proteins/ultrastructure , Myocardium/metabolism , Peptide Fragments/chemistry , Peptide Fragments/ultrastructure , Protein Kinases/chemistry , Protein Kinases/ultrastructure , Computer Simulation , Connectin , Humans , Microscopy, Atomic Force/methods , Protein Conformation , Refractometry/methods
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