TY - JOUR
T1 - Liquid-Liquid Phase Separation of the Intrinsically Disordered Domain of the Fused in Sarcoma Protein Results in Substantial Slowing of Hydration Dynamics
AU - Krevert, Carola S.
AU - Chavez, Daniel
AU - Chatterjee, Sayantan
AU - Stelzl, Lukas S.
AU - Pütz, Sabine
AU - Roeters, Steven J.
AU - Rudzinski, Joseph F.
AU - Fawzi, Nicolas L.
AU - Girard, Martin
AU - Parekh, Sapun H.
AU - Hunger, Johannes
PY - 2023/12/14
Y1 - 2023/12/14
N2 - Formation of liquid condensates plays a critical role in biology via localization of different components or via altered hydrodynamic transport, yet the hydrogen-bonding environment within condensates, pivotal for solvation, has remained elusive. We explore the hydrogen-bond dynamics within condensates formed by the low-complexity domain of the fused in sarcoma protein. Probing the hydrogen-bond dynamics sensed by condensate proteins using two-dimensional infrared spectroscopy of the protein amide I vibrations, we find that frequency-frequency correlations of the amide I vibration decay on a picosecond time scale. Interestingly, these dynamics are markedly slower for proteins in the condensate than in a homogeneous protein solution, indicative of different hydration dynamics. All-atom molecular dynamics simulations confirm that lifetimes of hydrogen-bonds between water and the protein are longer in the condensates than in the protein in solution. Altered hydrogen-bonding dynamics may contribute to unique solvation and reaction dynamics in such condensates.
AB - Formation of liquid condensates plays a critical role in biology via localization of different components or via altered hydrodynamic transport, yet the hydrogen-bonding environment within condensates, pivotal for solvation, has remained elusive. We explore the hydrogen-bond dynamics within condensates formed by the low-complexity domain of the fused in sarcoma protein. Probing the hydrogen-bond dynamics sensed by condensate proteins using two-dimensional infrared spectroscopy of the protein amide I vibrations, we find that frequency-frequency correlations of the amide I vibration decay on a picosecond time scale. Interestingly, these dynamics are markedly slower for proteins in the condensate than in a homogeneous protein solution, indicative of different hydration dynamics. All-atom molecular dynamics simulations confirm that lifetimes of hydrogen-bonds between water and the protein are longer in the condensates than in the protein in solution. Altered hydrogen-bonding dynamics may contribute to unique solvation and reaction dynamics in such condensates.
UR - https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85180005283&origin=inward
UR - https://www.ncbi.nlm.nih.gov/pubmed/38056002
U2 - 10.1021/acs.jpclett.3c02790
DO - 10.1021/acs.jpclett.3c02790
M3 - Article
C2 - 38056002
SN - 1948-7185
VL - 14
SP - 11224
EP - 11234
JO - Journal of Physical Chemistry Letters
JF - Journal of Physical Chemistry Letters
IS - 49
ER -