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Properties of a tardigrade desiccation-tolerance protein aerogel

https://doi.org/10.1016/j.bpj.2023.05.002

Eicher, Jonathan ; Hutcheson, Brent O. ; Pielak, Gary J. ( June 2023 , Biophysical Journal)

Free, publicly-accessible full text available June 1, 2024
Using NMR-detected hydrogen-deuterium exchange to quantify protein stability in cosolutes, under crowded conditions in vitro and in cells

https://doi.org/10.1016/j.mrl.2023.04.003

Chu, I-Te ; Pielak, Gary J. ( May 2023 , Magnetic Resonance Letters)

Free, publicly-accessible full text available May 1, 2024
How Sugars Protect Dry Protein Structure

https://doi.org/10.1021/acs.biochem.2c00692

Brom, Julia A. ; Petrikis, Ruta G. ; Pielak, Gary J. ( March 2023 , Biochemistry)

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Disordered proteins mitigate the temperature dependence of site-specific binding free energies

https://doi.org/10.1016/j.jbc.2023.102984

Thole, Joseph F. ; Waudby, Christopher A. ; Pielak, Gary J. ( March 2023 , Journal of Biological Chemistry)

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Macromolecular Crowding by Polyethylene Glycol Reduces Protein Breathing

https://doi.org/10.1021/acs.jpclett.3c00271

Chu, I-Te ; Hutcheson, Brent O. ; Malsch, Hudson R. ; Pielak, Gary J. ( March 2023 , The Journal of Physical Chemistry Letters)

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Secondary structure and stability of a gel‐forming tardigrade desiccation‐tolerance protein

https://doi.org/10.1002/pro.4495

Eicher, Jonathan E. ; Brom, Julia A. ; Wang, Shikun ; Sheiko, Sergei S. ; Atkin, Joanna M. ; Pielak, Gary J. ( December 2022 , Protein Science)

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Buffers, Especially the Good Kind

https://doi.org/10.1021/acs.biochem.1c00200

Pielak, Gary J. ( November 2021 , Biochemistry)

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A Difference between In Vitro and In-Cell Protein Dimer Formation

https://doi.org/10.1021/acs.biochem.1c00780

Chu, I-Te ; Stewart, Claire J. ; Speer, Shannon L. ; Pielak, Gary J. ( March 2022 , Biochemistry)

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Dynamical spectroscopy and microscopy of proteins in cells

https://doi.org/10.1016/j.sbi.2021.02.001

Gruebele, Martin ; Pielak, Gary J ( October 2021 , Current Opinion in Structural Biology)
null (Ed.)
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Trifluoroethanol and the behavior of a tardigrade desiccation‐tolerance protein

https://doi.org/10.1002/pro.4716

Wang, Shikun ; Eicher, Jonathan ; Pielak, Gary J. ( July 2023 , Protein Science)

Abstract
The cosolvent 2,2,2‐trifluoroethanol (TFE) is often used to mimic protein desiccation. We assessed the effects of TFE on cytosolic abundant heat soluble protein D (CAHS D) from tardigrades. CAHS D is a member of a unique protein class that is necessary and sufficient for tardigrades to survive desiccation. We find that the response of CAHS D to TFE depends on the concentration of both species. Dilute CAHS D remains soluble and, like most proteins exposed to TFE, gains α‐helix. More concentrated solutions of CAHS D in TFE accumulate β‐sheet, driving both gel formation and aggregation. At even higher TFE and CAHS D concentrations, samples phase separate without aggregation or increases in helix. Our observations show the importance of considering protein concentration when using TFE.

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