Use of Protein Thin Film Organized by External Electric Field as a Template for Protein Crystallization.

The well-known difficulty to obtain high-quality protein crystals has motivated researchers to come up with new methods or modifications of established crystallization methods to stimulate the growth of good diffracting crystals. In the present work, a new approach, using a protein thin film organized by external electric field (EEF) as a template for protein crystal growth, is introduced. This method increased nucleation of hen egg white lysozyme (HEWL) in comparison with the classical vapor diffusion method, besides improving crystal morphology and size.

Oral Health Literacy and Retention of Health Information Among Pregnant Women: A Randomised Controlled Trial.

Purpose: This study evaluated the effect of oral health literacy (OHL) on the retention of health information in pregnant women.

Materials And Methods: A total of 175 pregnant women were randomly assigned to standard oral (spoken), written and control intervention groups. With the exception of the control group, the interventions investigated the eating habits and oral hygiene among children under 2 years of age.

Salivary detection of periodontopathic bacteria in Fanconi's anemia patients.

Fanconi's anemia (FA) is characterized by bone marrow failure and can lead to infections such as periodontal disease. The aim of this study was to compare the prevalence of four periodontopathic bacteria including Aggregatibacter actinomycetemcomitans, Porphyromonas gingivalis, Fusobacterium nucleatum and Treponema denticola in saliva samples from children with and without FA. Paraffin-stimulated saliva samples were collected from 71 children and adolescents, aged 6-18 years old.

Effect of protein solution components in the adsorption of Herbaspirillum seropedicae GlnB protein on mica.

The adsorption of proteins and its buffer solution on mica surfaces was investigated by atomic force microscopy (AFM). Different salt concentration of the Herbaspirillum seropedicae GlnB protein (GlnB-Hs) solution deposited on mica was investigated. This protein is a globular, soluble homotrimer (36kDa), member of PII-like proteins family involved in signal transducing in prokaryote.

Purification and characterization of the bifunctional uridylyltransferase and the signal transducing proteins GlnB and GlnK from Herbaspirillum seropedicae.

GlnD is a bifunctional uridylyltransferase/uridylyl-removing enzyme that has a central role in the general nitrogen regulatory system NTR. In enterobacteria, GlnD uridylylates the PII proteins GlnB and GlnK under low levels of fixed nitrogen or ammonium. Under high ammonium levels, GlnD removes UMP from these proteins (deuridylylation).

Purification and characterisation of Azospirillum brasilense N-truncated NtrX protein.

The NtrX protein has been identified as a transcriptional activator of genes involved in the metabolic control of alternative nitrogen sources, acting as a member of a two-component regulatory system. The in silico analysis of the NtrX amino acid sequence shows that this protein contains an N-terminal receiver domain, a central AAA+ superfamily domain and a C-terminal DNA binding domain. To over-express and purify this protein, the ntrX gene of Azospirillum brasilense lacking the first eight codons was cloned into the vector pET29a+.

Effect of T- and C-loop mutations on the Herbaspirillum seropedicae GlnB protein in nitrogen signalling.

Proteins of the PII family are found in species of all kingdoms. Although these proteins usually share high identity, their functions are specific to the different organisms. Comparison of structural data from Escherichia coli GlnB and GlnK and Herbaspirillum seropedicae GlnB showed that the T-loop and C-terminus were variable regions.

In vitro uridylylation of the Azospirillum brasilense N-signal transducing GlnZ protein.

Azospirillum brasilense is a diazotroph which associates with important agricultural crops. The nitrogen fixation process in this organism is highly regulated by ammonium and oxygen, and involves several proteins including the two PII-like proteins, GlnB and GlnZ. Although these proteins are structurally very similar, they play different roles in the control of nitrogen fixation.