BROWSE

Related Researcher

Author's Photo

Kwak, Sang Kyu
Kyu’s MolSim Lab @ UNIST
Research Interests
  • Molecular modeling and simulation, statistical thermodynamics, molecular physics

ITEM VIEW & DOWNLOAD

Hydrogen‐Bond Free Energy of Local Biological Water

DC Field Value Language
dc.contributor.author Park, Won-Woo ko
dc.contributor.author Lee, Kyung Min ko
dc.contributor.author Lee, Byeong Sung ko
dc.contributor.author Kim, Young Jae ko
dc.contributor.author Joo, Se Hun ko
dc.contributor.author Kwak, Sang Kyu ko
dc.contributor.author Yoo, Tae Hyeon ko
dc.contributor.author Kwon, Oh-Hoon ko
dc.date.available 2020-03-04T07:09:12Z -
dc.date.created 2020-03-01 ko
dc.date.issued 2020-02 ko
dc.identifier.citation ANGEWANDTE CHEMIE-INTERNATIONAL EDITION ko
dc.identifier.issn 1433-7851 ko
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/31316 -
dc.description.abstract Here, we propose an experimental methodology based on femtosecond‐resolved fluorescence spectroscopy to measure the hydrogen (H)‐bond free energy of water at protein surfaces under isothermal conditions. A demonstration was conducted by installing a non‐canonical isostere of tryptophan (7‐azatryptophan) at the surface of a coiled‐coil protein to exploit the photoinduced proton transfer of its chromophoric moiety, 7‐azaindole. The H‐bond free energy of such biological water was evaluated by comparing the rates of the proton transfer, sensitive to the hydration environment, at the protein surface and in bulk water, and it was found to be higher than that of bulk water by 0.4 kcal/mol. The free‐energy difference is dominated by the entropic cost in the H‐bond network among water molecules at the hydrophilic and charged protein surface. Our study opens a door to accessing the energetics and dynamics of local biological water to give insight its roles in protein structure and function. ko
dc.language 영어 ko
dc.publisher WILEY-V C H VERLAG GMBH ko
dc.title Hydrogen‐Bond Free Energy of Local Biological Water ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-85082601847 ko
dc.identifier.wosid 000522540300001 ko
dc.type.rims ART ko
dc.identifier.doi 10.1002/ange.202002025 ko
dc.identifier.url https://onlinelibrary.wiley.com/doi/10.1002/ange.202002025 ko
Appears in Collections:
PHY_Journal Papers
ECHE_Journal Papers

find_unist can give you direct access to the published full text of this article. (UNISTARs only)

Show simple item record

qrcode

  • mendeley

    citeulike

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

MENU