Do osmolytes impact the structure and dynamics of myoglobin?

Dorota Kossowska, Kyungwon Kwak, Minhaeng Cho

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


Osmolytes are small organic compounds that can affect the stability of proteins in living cells. The mechanism of osmolytes’ protective effects on protein structure and dynamics has not been fully explained, but in general, two possibilities have been suggested and examined: a direct interaction of osmolytes with proteins (water replacement hypothesis), and an indirect interaction (vitrification hypothesis). Here, to investigate these two possible mechanisms, we studied myoglobin-osmolyte systems using FTIR, UV-vis, CD, and femtosecond IR pump-probe spectroscopy. Interestingly, noticeable changes are observed in both the lifetime of the CO stretch of CO-bound myoglobin and the spectra of UV-vis, CD, and FTIR upon addition of the osmolytes. In addition, the temperature-dependent CD studies reveal that the protein’s thermal stability depends on molecular structure, hydrogen-bonding ability, and size of osmolytes. We anticipate that the present experimental results provide important clues about the complicated and intricate mechanism of osmolyte effects on protein structure and dynamics in a crowded cellular environment.

Original languageEnglish
Article number3189
Issue number12
Publication statusPublished - 2018 Dec 3

Bibliographical note

Publisher Copyright:
© 2018 by the authors.


  • IR probe
  • IR pump-probe
  • IR spectroscopy
  • Myoglobin
  • Myoglobin
  • Osmolytes
  • Protein dynamics
  • Ultrafast vibrational dynamics
  • Vibrational probe
  • Vibrational spectroscopy

ASJC Scopus subject areas

  • Analytical Chemistry
  • Chemistry (miscellaneous)
  • Molecular Medicine
  • Pharmaceutical Science
  • Drug Discovery
  • Physical and Theoretical Chemistry
  • Organic Chemistry


Dive into the research topics of 'Do osmolytes impact the structure and dynamics of myoglobin?'. Together they form a unique fingerprint.

Cite this