Abstract
Local probes are indispensable to study protein structure and dynamics with site-specificity. The isonitrile functional group is a highly sensitive and H-bonding interaction-specific probe. Isonitriles exhibit large spectral shifts and transition dipole moment changes upon H-bonding while being weakly affected by solvent polarity. These unique properties allow a clear separation of distinct subpopulations of interacting species and an elucidation of their ultrafast dynamics with two-dimensional infrared (2D-IR) spectroscopy. Here, we apply 2D-IR to quantify the picosecond chemical exchange dynamics of solute-solvent complexes forming between isonitrile-derivatized alanine and fluorinated ethanol, where the degree of fluorination controls their H-bond-donating ability. We show that the molecules undergo faster exchange in the presence of more acidic H-bond donors, indicating that the exchange process is primarily dependent on the nature of solvent-solvent interactions. We foresee isonitrile as a highly promising probe for studying of H-bonds dynamics in the active site of enzymes.
| Original language | English |
|---|---|
| Pages (from-to) | 7878-7883 |
| Number of pages | 6 |
| Journal | Journal of Physical Chemistry Letters |
| Volume | 10 |
| Issue number | 24 |
| DOIs | |
| Publication status | Published - 2019 Dec 19 |
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ASJC Scopus subject areas
- Materials Science(all)
- Physical and Theoretical Chemistry
Cite this
Ultrafast Chemical Exchange Dynamics of Hydrogen Bonds Observed via Isonitrile Infrared Sensors : Implications for Biomolecular Studies. / Kübel, Joachim; Lee, Giseong; Ooi, Saik Ann; Westenhoff, Sebastian; Han, Hogyu; Cho, Minhaeng; Maj, Michał.
In: Journal of Physical Chemistry Letters, Vol. 10, No. 24, 19.12.2019, p. 7878-7883.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Ultrafast Chemical Exchange Dynamics of Hydrogen Bonds Observed via Isonitrile Infrared Sensors
T2 - Implications for Biomolecular Studies
AU - Kübel, Joachim
AU - Lee, Giseong
AU - Ooi, Saik Ann
AU - Westenhoff, Sebastian
AU - Han, Hogyu
AU - Cho, Minhaeng
AU - Maj, Michał
PY - 2019/12/19
Y1 - 2019/12/19
N2 - Local probes are indispensable to study protein structure and dynamics with site-specificity. The isonitrile functional group is a highly sensitive and H-bonding interaction-specific probe. Isonitriles exhibit large spectral shifts and transition dipole moment changes upon H-bonding while being weakly affected by solvent polarity. These unique properties allow a clear separation of distinct subpopulations of interacting species and an elucidation of their ultrafast dynamics with two-dimensional infrared (2D-IR) spectroscopy. Here, we apply 2D-IR to quantify the picosecond chemical exchange dynamics of solute-solvent complexes forming between isonitrile-derivatized alanine and fluorinated ethanol, where the degree of fluorination controls their H-bond-donating ability. We show that the molecules undergo faster exchange in the presence of more acidic H-bond donors, indicating that the exchange process is primarily dependent on the nature of solvent-solvent interactions. We foresee isonitrile as a highly promising probe for studying of H-bonds dynamics in the active site of enzymes.
AB - Local probes are indispensable to study protein structure and dynamics with site-specificity. The isonitrile functional group is a highly sensitive and H-bonding interaction-specific probe. Isonitriles exhibit large spectral shifts and transition dipole moment changes upon H-bonding while being weakly affected by solvent polarity. These unique properties allow a clear separation of distinct subpopulations of interacting species and an elucidation of their ultrafast dynamics with two-dimensional infrared (2D-IR) spectroscopy. Here, we apply 2D-IR to quantify the picosecond chemical exchange dynamics of solute-solvent complexes forming between isonitrile-derivatized alanine and fluorinated ethanol, where the degree of fluorination controls their H-bond-donating ability. We show that the molecules undergo faster exchange in the presence of more acidic H-bond donors, indicating that the exchange process is primarily dependent on the nature of solvent-solvent interactions. We foresee isonitrile as a highly promising probe for studying of H-bonds dynamics in the active site of enzymes.
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U2 - 10.1021/acs.jpclett.9b03144
DO - 10.1021/acs.jpclett.9b03144
M3 - Article
C2 - 31794222
AN - SCOPUS:85076560007
VL - 10
SP - 7878
EP - 7883
JO - Journal of Physical Chemistry Letters
JF - Journal of Physical Chemistry Letters
SN - 1948-7185
IS - 24
ER -