We calculate isotope mass shift for several light ions using Dirac wave functions and mass shift operator with relativistic corrections of the order of (αZ) 2 . Calculated relativistic corrections to the specific mass shift vary from a fraction of a percent for Carbon, to 2% for Magnesium. Relativistic corrections to the normal mass shift are typically smaller. Interestingly, the final relativistic mass shifts for the levels of one multiplet appear to be even closer than for non-relativistic operator. That can be important for the astrophysical search for possible α-variation, where isotope shift is a source of important systematic error. Our calculations show that for levels of the same multiplet this systematics is negligible and they can be used as probes for α-variation.

At present several groups are analyzing astrophysical data in a search for the time variation of the finestructure constant ␣. Here we discuss how to exclude systematic effects caused by changes in the isotope abundances during the evolution of the universe. We suggest using particular combinations of the transition frequencies of O II, Al II, Al III, Si II, and Mn II as anchors, which are insensitive to ␣ variation and to changes in isotope abundances. These anchors can be used to determine the cosmological redshift. Then, one can use other combinations of frequencies as probes for the time variation of ␣ and another set as probes for the isotopic abundances. In this way it is possible to eliminate one source of systematic errors in the search for ␣ variation and get more information about evolution of the isotopes. On the level of accuracy that has already been reached in the search for ␣ variation it is possible to see ϳ10% changes in isotope abundances of Si and Ni.

Various biochemical and biophysical processes, occurring on multiple time and length scales, can nowadays be studied using specialized software packages on supercomputer clusters. The complexity of such simulations often requires application of different methods in a single study and strong computational expertise. We have developed VIKING, a convenient web platform for carrying out multiscale computations on supercomputers. VIKING allows combining methods in standardized workflows, making complex simulations accessible to a broader biochemical and biophysical society.

We are introducing Pep McConst—a software that employs a Monte‐Carlo algorithm to construct 3D structures of polypeptide chains which could subsequently be studied as stand‐alone macromolecules or complement the structure of known proteins. Using an approach to avoid steric clashes, Pep McConst allows to create multiple structures for a predefined primary sequence of amino acids. These structures could then effectively be used for further structural analysis and investigations. The article introduces the algorithm and describes its user‐friendly approach that was made possible through the VIKING online platform. Finally, the manuscript provides several highlight examples where Pep McConst was used to predict the structure of the C‐terminal of a known protein, generate a missing bit of already crystallized protein structures and simply generate short polypeptide chains.