TY - JOUR
T1 - Effect of Osmolytes on Water Mobility Correlates with Their Stabilizing Effect on Proteins
AU - Hishida, Mafumi
AU - Anjum, Rubaiya
AU - Anada, Takahisa
AU - Murakami, Daiki
AU - Tanaka, Masaru
N1 - Funding Information:
This work was supported by JSPS KAKENHI (Grant Nos. JP19H05717 to M.H. and JP19H05720 to M.T.). We are also thankful to the Cooperative Research Program “Dynamic Alliance for Open Innovation Bridging Human, Environment, and Materials”.
Publisher Copyright:
© 2022 American Chemical Society.
PY - 2022/4/7
Y1 - 2022/4/7
N2 - There is a long, ongoing debate on how small molecules (osmolytes) affect the stability of proteins. The present study found that change in collective rotational dynamics of water in osmolyte solutions likely has a dominant effect on protein denaturation. According to THz spectroscopy analysis, osmolytes that stabilize proteins are accompanied by bound hydration water with slow dynamics, while the collective rotational dynamics of water is accelerated in the case of denaturant osmolytes. Among 15 osmolytes studied here, there is a good correlation between the change in mobility in terms of water rotational dynamics and the denaturation temperature of ribonuclease A. The changes in water dynamics due to osmolytes can be regarded as a pseudo-temperature-change, which agrees well with the change in protein denaturation temperature. These results indicate that the molecular dynamics of water around the protein is a key factor for protein denaturation.
AB - There is a long, ongoing debate on how small molecules (osmolytes) affect the stability of proteins. The present study found that change in collective rotational dynamics of water in osmolyte solutions likely has a dominant effect on protein denaturation. According to THz spectroscopy analysis, osmolytes that stabilize proteins are accompanied by bound hydration water with slow dynamics, while the collective rotational dynamics of water is accelerated in the case of denaturant osmolytes. Among 15 osmolytes studied here, there is a good correlation between the change in mobility in terms of water rotational dynamics and the denaturation temperature of ribonuclease A. The changes in water dynamics due to osmolytes can be regarded as a pseudo-temperature-change, which agrees well with the change in protein denaturation temperature. These results indicate that the molecular dynamics of water around the protein is a key factor for protein denaturation.
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U2 - 10.1021/acs.jpcb.1c10634
DO - 10.1021/acs.jpcb.1c10634
M3 - Article
C2 - 35349285
AN - SCOPUS:85127905868
SN - 1520-6106
VL - 126
SP - 2466
EP - 2475
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
IS - 13
ER -