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Chemical communications (Cambridge, England)2010; 47(1); 289-291; doi: 10.1039/c0cc01817a

Direct observation of myoglobin structural dynamics from 100 picoseconds to 1 microsecond with picosecond X-ray solution scattering.

Abstract: Here we report structural dynamics of equine myoglobin (Mb) in response to the CO photodissociation visualized by picosecond time-resolved X-ray solution scattering. The data clearly reveal new structural dynamics that occur in the timescale of ∼360 picoseconds (ps) and ∼9 nanoseconds (ns), which have not been clearly detected in previous studies.
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Publication Date: 2010-08-24 PubMed ID: 20733999PubMed Central: PMC2999690DOI: 10.1039/c0cc01817aGoogle Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research paper investigates the structural dynamics of myoglobin, a type of protein in muscle tissues, in response to carbon monoxide photodissociation, using a technique known as picosecond time-resolved X-ray solution scattering. The study finds new structural changes in the protein on the picosecond and nanosecond timescales that were not identified in prior research.

Introduction and Methodology

  • The research focuses on understanding the structural dynamics of equine myoglobin, an oxygen-binding protein present in horse muscle tissues. Myoglobin’s function relates to oxygen storage and delivery in muscles.
  • The investigation is triggered by carbon monoxide photodissociation – essentially the breaking down of carbon monoxide molecules using light.
  • To visualize these dynamics, the researchers use a technique known as picosecond time-resolved X-ray solution scattering. This advanced method allows for observations of structural changes in molecules on extremely short time scales – up to one trillionth (picosecond) of a second.

Results: Novel Structural Dynamics

  • The key findings of this research are new structural dynamics, or changes, within the myoglobin on timescales of approximately 360 picoseconds and 9 nanoseconds.
  • These timescales are incredibly short, with one picosecond being a trillionth of a second and a nanosecond being a billionth of a second. The detection of changes on these scales demonstrates the sensitivity of the picosecond X-ray solution scattering technique.
  • Such rapid structural changes had not been clearly detected in previous myoglobin studies, underscoring the novelty of these findings.

Implications of the Research

  • This novel observation can potentially contribute to the broader understanding of protein dynamics in general and the specific function and behavior of myoglobin.
  • Given the instrumental role of myoglobin in oxygen storage and delivery in muscles, insights from this research may have potential implications in muscular disease study, sports science, and other related areas.
  • More broadly, the demonstration of the picosecond time-resolved X-ray solution scattering technique’s effectiveness in identifying subtle and rapid changes at molecular level can promote its application in various other areas of scientific research.

Cite This Article

APA
Kim KH, Oang KY, Kim J, Lee JH, Kim Y, Ihee H. (2010). Direct observation of myoglobin structural dynamics from 100 picoseconds to 1 microsecond with picosecond X-ray solution scattering. Chem Commun (Camb), 47(1), 289-291. https://doi.org/10.1039/c0cc01817a

Publication

Chemical communications (Cambridge, England)
ISSN: 1364-548X
NlmUniqueID: 9610838
Country: England
Language: English
Volume: 47
Issue: 1
Pages: 289-291

Researcher Affiliations

Kim, Kyung Hwan
  • Center for Time-Resolved Diffraction, Department of Chemistry, Graduate School of Nanoscience & Technology (WCU), KAIST, Daejeon 305-701, Korea.
Oang, Key Young
    Kim, Jeongho
      Lee, Jae Hyuk
        Kim, Youngmin
          Ihee, Hyotcherl

            MeSH Terms

            • Carbon Monoxide / chemistry
            • Myoglobin / chemistry
            • Photochemistry
            • Protein Conformation
            • Scattering, Small Angle
            • Solutions
            • Thermodynamics
            • Time Factors
            • X-Ray Diffraction

            Grant Funding

            • P41 RR007707 / NCRR NIH HHS
            • P41 RR007707-12 / NCRR NIH HHS
            • RR007707 / NCRR NIH HHS

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            Citations

            This article has been cited 19 times.
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