draeger-lab/C_striatum_wetlab: Article

<p>This release corresponds to making this repository public upon the acceptance of the manuscript. The full article can be found <a href="https://www.frontiersin.org/articles/10.3389/fbinf.2023.1214074/full">here</a>.</p&gt

draeger-lab/C_striatum_GEMs: Article

<p>This release corresponds to making this repository public upon the acceptance of the manuscript. The full article can be found <a href="https://www.frontiersin.org/articles/10.3389/fbinf.2023.1214074/full">here</a>.</p&gt

refineGEMs

<p>With this release, the following files are updated:</p> <ul> <li>README</li> <li>Makefile and make.bat</li> <li>requirements.txt</li> <li>main.py</li> </ul> <p>For the documentation to work, a <code>requirements.in</code> file was created to automatically update the <code>requirements.txt</code> to make it more reproducible. Furthermore, the documentation for the 'Notes for developers' section is updated, and minor bugs in the <code>main.py</code> file are fixed.</p>If you use refineGEMs, please cite it as below

Molecular Flexibility of Antibodies Preserved Even in the Dense Phase after Macroscopic Phase Separation

Antibody therapies are typically based on high-concentration formulations that need to be administered subcutaneously. These conditions induce several challenges, inter alia a viscosity suitable for injection, sufficient solution stability, and preservation of molecular function. To obtain systematic insights into the molecular factors, we study the dynamics on the molecular level under strongly varying solution conditions. In particular, we use solutions of antibodies with poly(ethylene glycol), in which simple cooling from room temperature to freezing temperatures induces a transition from a well-dispersed solution into a phase-separated and macroscopically arrested system. Using quasi-elastic neutron scattering during in situ cooling ramps and in prethermalized measurements, we observe a strong decrease in antibody diffusion, while internal flexibility persists to a significant degree, thus ensuring the movement necessary for the preservation of molecular function. These results are relevant for a more dynamic understanding of antibodies in high-concentration formulations, which affects the formation of transient clusters governing the solution viscosity