Picosecond Polarization Studies of Protein Relaxation

  • Xiaoliang Xie
  • J. D. Simon
Conference paper
Part of the Springer Series in Chemical Physics book series (CHEMICAL, volume 53)


Protein relaxation in myoglobin (Mb) following the photoelimination of CO from carbonmonoxymyoglobin (MbCO) is examined using picosecond time resolved circular dichroism (CD) and magnetic circular dichroism (MCD) spectroscopies. The transient CD signal reveals a relaxation process which requires several hundred picoseconds. Comparison with optical absorption studies on the Q-band and near infrared absorption of Mb and linear dichroism studies of the Soret optical absorptions suggest that the CD dynamics reflect a conformation relaxation of the surrounding protein structure.


Circular Dichroism Circular Dichroism Spectrum Probe Pulse Transient Absorption Magnetic Circular Dichroism 
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Copyright information

© Springer-Verlag Berlin, Heidelberg 1990

Authors and Affiliations

  • Xiaoliang Xie
    • 1
  • J. D. Simon
    • 1
  1. 1.Department of ChemistryUniversity of California at San DiegoLa JollaUSA

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