RESUMO
Nondestructive magnetic measurement methods can be successfully applied to determine the embrittlement of nuclear pressure vessel steel caused by neutron irradiation. It was found in previous works that reasonable correlation could be obtained between the nondestructively measured magnetic parameters and destructively determined ductile-to-brittle transition temperature. However, a large scatter of the measurement points was detected even in the cases of the non-irradiated reference samples. The reason for their scattering was attributed to the local inhomogeneity of material. This conclusion is verified in the present work by applying three different magnetic methods on two sets of Charpy samples made of two different reactor steel materials. It was found that by an optimal magnetic pre-selection of samples, a good, linear correlation can be found between magnetic parameters as well as the ductile-to-brittle transition temperature with low scattering of points. This result shows that neutron irradiation embrittlement depends very much on the local material properties.
RESUMO
ANTIC ALIGN: is an interactive software developed to simultaneously visualize, analyze and modify alignments of DNA and/or protein sequences that arise during combinatorial protein engineering, design and selection. ANTIC ALIGN: combines powerful functions known from currently available sequence analysis tools with unique features for protein engineering, in particular the possibility to display and manipulate nucleotide sequences and their translated amino acid sequences at the same time. ANTIC ALIGN: offers both template-based multiple sequence alignment (MSA), using the unmutated protein as reference, and conventional global alignment, to compare sequences that share an evolutionary relationship. The application of similarity-based clustering algorithms facilitates the identification of duplicates or of conserved sequence features among a set of selected clones. Imported nucleotide sequences from DNA sequence analysis are automatically translated into the corresponding amino acid sequences and displayed, offering numerous options for selecting reading frames, highlighting of sequence features and graphical layout of the MSA. The MSA complexity can be reduced by hiding the conserved nucleotide and/or amino acid residues, thus putting emphasis on the relevant mutated positions. ANTIC ALIGN: is also able to handle suppressed stop codons or even to incorporate non-natural amino acids into a coding sequence. We demonstrate crucial functions of ANTIC ALIGN: in an example of Anticalins selected from a lipocalin random library against the fibronectin extradomain B (ED-B), an established marker of tumor vasculature. Apart from engineered protein scaffolds, ANTIC ALIGN: provides a powerful tool in the area of antibody engineering and for directed enzyme evolution.