Disentangling the complexity of low complexity proteins.

Unlabelled: There are multiple definitions for low complexity regions (LCRs) in protein sequences, with all of them broadly considering LCRs as regions with fewer amino acid types compared to an average composition. Following this view, LCRs can also be defined as regions showing composition bias. In this critical review, we focus on the definition of sequence complexity of LCRs and their connection with structure.

[On the occasion of the 20th anniversary of the accident on the Chernobyl NPP: medical consequences in Armenia].

The aim of this work is the analysis of the indices of the health and of the structure of the sicknesses of the inhabitants of Armenia who took part in the liquidation of the consequences of the Chernobyl accident. Also it is the determination of possible dependence of the frequency of diseases for the most widespread classes of sicknesses on the received dose of the irradiation, according to the data of the clinical examination and dispensarysation; and also it is the revelation of the role of other factors influenced on the health indexes.

Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA.

The stability of protein is defined not only by the hydrogen bonding, hydrophobic effect, van der Waals interactions, and salt bridges. Additional, much more subtle contributions to protein stability can arise from surface residues that change their properties upon unfolding. The recombinant major cold shock protein of Escherichia coli CspA an all-beta protein unfolds reversible in a two-state manner, and behaves in all other respects as typical globular protein.

Mutagenesis disrupts posttranslational processing of the Na,K-ATPase catalytic subunit.

The first 5 amino acids of the catalytic alpha 1 isoform from Na,K-ATPase are cleaved enzymatically during or after translation. To evaluate the structural requirements for that cleavage, we constructed amino-terminal mutants of alpha 1 in which an epitope tag from the c-myc oncogene product was added. Immunoblots of isolated membranes from transfected monkey kidney cells revealed binding of an antibody specific for the first 9 residues of the alpha 1 nascent protein.