The microstructure of the starch from the underutilized seed of jaboticaba (Plinia cauliflora).

This work presents a starch extracted from jaboticaba seeds. The extraction yielded 22.65 ± 0.

Determination of specific and non-specific protein-protein interactions for beta-lactoglobulin by analytical ultracentrifugation and membrane osmometry experiments.

Protein-protein interactions are essential for the understanding of biological processes. Specific protein aggregation is an important aspect for many biological systems. In particular, electrostatic interactions play the key role for protein-protein interactions, as many amino acids have pH-dependent charge states.

Influence of Levan on the Thermally Induced Gel Formation of β-Lactoglobulin.

In this study, the influence of levan on the phase behavior and the thermally induced gelation of the mixed β-lactoglobulin-levan gels as a function of polymer content, molecular weight and ionic strength was characterized. For this purpose, rheology was used to study the mechanical properties of the gels and the water binding of the network structure was investigated by time domain nuclear magnetic resonance. Phase behavior and network type were analyzed by optical observation and electron microscopy.

Molecular weight dependent structure of the exopolysaccharide levan.

Levan is a bacterial homopolysaccharide, which consists of β-2➔6 linked β-(D)-fructose monomers. Because of its structural properties and its health promoting effects, levan is a promising functional ingredient for food, cosmetic and pharmaceutical products. The properties of levan have been reported to be linked to its molecular weight.

Size-Dependent Variability in Flow and Viscoelastic Behavior of Levan Produced by TMW 2.1191.

Levan is a fructan-type exopolysaccharide which is produced by many microbes from sucrose via extracellular levansucrases. The hydrocolloid properties of levan depend on its molecular weight, while it is unknown why and to what extent levan is functionally diverse depending on its size. The aim of our study was to gain deeper insight into the size-dependent functional variability of levan.

Calmodulin regulates dimerization, motility, and lipid binding of Leishmania myosin XXI.

Myosin XXI is the only myosin expressed in Leishmania parasites. Although it is assumed that it performs a variety of motile functions, the motor's oligomerization states, cargo-binding, and motility are unknown. Here we show that binding of a single calmodulin causes the motor to adopt a monomeric state and to move actin filaments.

Cloning, expression, and characterization of a novel molecular motor, Leishmania myosin-XXI.

The genome of the Leishmania parasite contains two classes of myosin. Myosin-XXI, seemingly the only myosin isoform expressed in the protozoan parasite, has been detected in both the promastigote and amastigote stages of the Leishmania life cycle. It has been suggested to perform a variety of functions, including roles in membrane anchorage, but also long-range directed movements of cargo.

Molecular architecture: construction of self-assembled organophosphonate duplexes and their electrochemical characterization.

Self-assembled monolayers of phosphonates (SAMPs) of 11-hydroxyundecylphosphonic acid, 2,6-diphosphonoanthracene, 9,10-diphenyl-2,6-diphosphonoanthracene, and 10,10'-diphosphono-9,9'-bianthracene and a novel self-assembled organophosphonate duplex ensemble were synthesized on nanometer-thick SiO(2)-coated, highly doped silicon electrodes. The duplex ensemble was synthesized by first treating the SAMP prepared from an aromatic diphosphonic acid to form a titanium complex-terminated one; this was followed by addition of a second equivalent of the aromatic diphosphonic acid. SAMP homogeneity, roughness, and thickness were evaluated by AFM; SAMP film thickness and the structural contributions of each unit in the duplex were measured by X-ray reflection (XRR).