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5 publications that put protein quality checks into the workflow, using Tycho

2 min read
Mar 19, 2020
Tycho instrument

Tycho launched a little over two years ago in January 2018 as the solution for quickly assessing protein quality. Soon after, The Scientist journal even recognized Tycho as one of the top 10 innovations of 2018.

By providing a better understanding of the quality of their samples, Tycho continues to help prevent unnecessary experiments, minimize questionable data, and change how scientists approach experiments.

Here is a sampling of five recent publications from scientists who use Tycho to check the quality of their protein samples.

1. Human and mouse albumin bind their respective neonatal Fc receptors differently Nilsen et al., Scientific Reports, 8:14648 (2018).
Drugs that use serum albumin as a carrier protein are protected from degradation, in part, due to interactions with the FcRn receptor protein. This study pinpoints key structural features in human and mouse albumins that impact the cross-species binding with FcRn.


2. Critical residues in the aminoglycoside-resistance 16S rRNA (m7G1405) methyltransferase RmtC play distinct roles in 30S substrate recognition, M.Nosrati et al., Journal of Biological Chemistry, 294: 17642 (2019).
Emory University researchers have identified important sites on the methyltransferase RmtC that allow it to bind with bacterial ribosomes and methylate 16S rRNA. Methylation of this rRNA subunit is associated with high-level antibiotic resistance.


3. Kinetic and structural analysis of human ALDH9A1, R. Končitíková et al., Bioscience Reports, 39:4 (2019).
ALDH9A1 is one of 19 aldehyde dehydrogenases produced in humans. By investigating the structure and enzyme kinetics of ALDH9A1, researchers have discovered a unique fold and position of a linker region not found in the other dehydrogenases.


4. Thermal unfolding and refolding of a lytic polysaccharide monooxygenase from Thermoascus aurantiacus, R. Singh, et al., RSC Advances, 9:51 (2019).
Scientists from the University of Copenhagen reveal interesting folding kinetics of a lytic polysaccharide monooxygenase (LPMO) enzyme, which has promising applications in degrading plant biomass.


5. Molecular basis for the binding and selective dephosphorylation of Na+/H+ exchanger 1 by calcineurin, R. Hendus-Altenburger et al., Nature Communications volume 10, 2019.
University of Copenhagen and University of Arizona researchers have revealed how calcineurin selectively dephosphorylates the human ion transporter NHE1, an important regulator of cellular pH and volume.


Do you think your experimental design can benefit from a quick check of protein sample quality?

Learn more about how Tycho can provide you an everyday solution, and more.