Screening of ligands for redox-active europium using magnetic resonance imaging.

We report a screening procedure to predict ligand coordination to Eu and Eu using magnetic resonance imaging in which bright images indicate complexation and dark images indicate no complexation. Here, paramagnetic Gd is used as a surrogate for Eu in the screening procedure to enable detection with magnetic resonance imaging. The screening procedure was tested using a set of eight ligands with known coordination to Eu and Eu, and results were found to be consistent with expected binding.

Learning about being a scientist from the vitamin B12 structure collaboration.

This historical note reviews the work that resulted in the publication of the structure of Vitamin B12 . The collaborations and resulting friendships that developed during this time made a strong impression on the author and encouraged her to pursue a scientific career.

Clinical correlation and molecular evaluation confirm that the MLH1 p.Arg182Gly (c.544A>G) mutation is pathogenic and causes Lynch syndrome.

Approximately 25 % of mismatch repair (MMR) variants are exonic nucleotide substitutions. Some result in the substitution of one amino acid for another in the protein sequence, so-called missense variants, while others are silent. The interpretation of the effect of missense and silent variants as deleterious or neutral is challenging.

Compensatory mutations in the L30e kink-turn RNA-protein complex.

The S. cerevisiae ribosomal protein L30e is an autoregulatory protein that binds to its own pre-mRNA and mature mRNA to inhibit splicing and translation, respectively. The L30e RNA-binding element is a stem-asymmetric loop-stem that forms a kink-turn.

Internal loop mutations in the ribosomal protein L30 binding site of the yeast L30 RNA transcript.

Yeast ribosomal protein L30 binds to an asymmetric, purine-rich internal loop in its transcript to repress its own splicing and translation. The protein-bound form of the stem-internal loop-stem RNA is an example of a kink-turn RNA structural motif. Analysis of kink-turn motifs reveals that in (2 + 5) internal loops, the identities of five nucleotides are very important, while the remaining two may be varied.

Inherent protein structural flexibility at the RNA-binding interface of L30e.

The Saccharomyces cerevisiae ribosomal protein L30 autoregulates its own expression by binding to a purine-rich internal loop in its pre-mRNA and mRNA. NMR studies of L30 and its RNA complex showed that both the internal loop of the RNA as well as a region of the protein become substantially more ordered upon binding. A crystal structure of a maltose binding protein (MBP)-L30 fusion protein with two copies in the asymmetric unit has been determined.