Miranda F. Mecha's research while affiliated with University of Wisconsin–Madison and other places

Publications (11)

Article
Correct protein folding is essential for the health and function of living organisms. Yet, it is not well understood how unfolded proteins reach their native state and avoid aggregation, especially within the cellular milieu. Some proteins, especially small, single-domain and apparent two-state folders, successfully attain their native state upon d...
Article
Low-concentration photochemically induced dynamic nuclear polarization (LC-photo-CIDNP) has recently emerged as an effective tool for the hyperpolarization of aromatic amino acids in solution, either in isolation or within proteins. One factor limiting the maximum achievable signal-to-noise ratio in LC-photo-CIDNP is the progressive degradation of...
Article
The relation between co- and post-translational protein folding and aggregation in the cell is poorly understood. Here, we employ a combination of fluorescence anisotropy decays in the frequency domain, fluorescence-detected solubility assays and NMR spectroscopy to explore the role of the ribosome in protein folding within a biologically relevant...
Article
Solution-state NMR typically requires 100 μM to 1 mM samples. This limitation prevents applications to mass-limited and aggregation-prone target molecules. Photochemically induced dynamic nuclear polarization was adapted to data collection on low-concentration samples by radiofrequency gating, enabling rapid 1D NMR spectral acquisition on aromatic...

Citations

... Fourth, hyperpolarization generation requires very little and cheap hardware and is quite mobile. The replacement of lasers by high-power LEDs for photo-CIDNP studies was successfully investigated by [39][40][41][42] and references therein. ...
... In addition, the ribosome is involved in mRNA-code recognition and proofreading [10][11][12] as well as in the control of translation rates via interactions with mRNA codons bearing high-and lowfrequency [13][14][15] and associated with variable tRNA abundance within the translation machinery [16][17][18]. Interestingly, the ribosome also assists de novo protein structure formation by minimizing cotranslational aggregation, thus increasing the yield of native-protein production [19,20]. The latter event, however, has not been shown to require --or even involve --direct interactions between the ribosome and the nascent protein chain. ...
... In both 1D and 2D MR techniques, valuable information can be obtained by changing the signal intensity or phase. Recently, advances have been made to detect even the smallest concentrations or amounts of substances [6,[42][43][44], but the focus in this study is more on investigating the feasibility of a background-free approach using 19 F NMR and 19 F MRI. ...