PubMed Health⌕ Search

PubMed · 14743530

[Glutamyl endopeptidase. Structure, function, practical use].

Abstract

Special features of the structural organization of serine proteases belonging to a new subfamily of glutamyl-specific endopeptidases, which possess an extremely strict substrate specificity, are discussed. Some areas of the practical application of these enzymes are considered. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2003, vol. 29, no. 6; see also http://www.maik.ru.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

E I Mil'gotina, T L Voiushina, G G Chestukhina. [Glutamyl endopeptidase. Structure, function, practical use].. https://doi.org/10.1023/b%3Arubi.0000008891.51576.d0

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

On the interpretation of residual dipolar couplings as reporters of molecular dynamics.

The analysis of residual dipolar couplings from an ensemble of conformations to extract molecular dynamics is intricate. The very mechanism that is necessary to perturb overall molecular tumbling to generate nonvanishing residual dipolar couplings gives rise to convoluted data. The measured values are essentially weighted averages over conformations. However, the weights are not simply the populations of conformations. Consequently, the observed order parameter is not exactly the true measure of motion. In the case of paramagnetic alignment, the apparent order parameter is expected to depend on the number of torsions that separate the locus of interest from the paramagnetic site. In the case of alignment due to steric obstruction, the uneven selection of conformations by their differing Saupe order matrices leads to a bias in the residual dipolar couplings-probed molecular dynamics.

Models, Molecular↗