Impact of calcium binding and thionylation of S100A1 protein on its nuclear magnetic resonance-derived structure and backbone dynamics.

S100 proteins play a crucial role in multiple important biological processes in vertebrate organisms acting predominantly as calcium signal transmitters. S100A1 is a typical representative of this family of proteins. After four Ca(2+) ions bind, it undergoes a dramatic conformational change, resulting in exposure, in each of its two identical subunits, a large hydrophobic cleft that binds to target proteins.

Solution NMR structure and dynamics of human apo-S100A1 protein.

S100A1 belongs to the EF-hand superfamily of calcium binding proteins. It is a representative of the S100 protein family based on amino acid sequence, three-dimensional structure, and biological function as a calcium signal transmitter. It is a homodimer of noncovalently bound subunits.

Population decline in Polish and Czech cities during post-socialism? Looking behind the official statistics.

The evolving debate on "urban shrinkage" mirrors an increasing interest in demographic phenomena on the part of urban scholars. This paper discusses ambiguous evidence about recent population decline in the large cities of Poland and the Czech Republic, with a particular focus on Łódz and Brno in general and their inner cities more specifically. By applying a mixed-method approach, the paper identifies indications of inner-city repopulation and socio-demographic diversification which are not yet apparent in register or census data.

Structural and motional changes induced in apo-S100A1 protein by the disulfide formation between its Cys 85 residue and beta-mercaptoethanol.

Recently, we have shown (Goch, G., Vdovenko, S., Kozłowska, H.

Free energy of helix propagation in short polyalanine chains determined from peptide growth simulations of La3+-binding model peptides. Comparison with experimental data.

Molecular dynamics (MD) is, at present, a unique tool making it possible to study, at the atomic level, conformational transitions in peptides and proteins. Nevertheless, because MD calculations are always based on a more or less approximate physical model, using a set of approximate parameters, their reliability must be tested by comparison with experimental data. Unfortunately, it is very difficult to find a peptide system in which conformational transitions can be studied both experimentally and using MD simulations so that a direct comparison of the results obtained in both ways could be made.