5 July 1989 Fast Structural Relaxations In Hemoglobin And Myoglobin: An Analysis Of Time Resolved Raman Studies
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Abstract
There was a time not too long ago when proteins were viewed as static structures. It is now apparent that proteins exhibit a wide variety of local and global dynamics; nevertheless, an understanding of both how proteins move and how these motions influence protein reactivity remains a fundamental, unanswered and illusive problem within biophysics. Most of the recent detailed studies to date have been theoretical endeavors utilizing molecular dynamics simulations. Unfortunately comparable experiments that are structurally specific or detailed are lacking. In this manuscript, several picosecond time resolved resonance Raman studies of hemoglobin and myoglobin are reviewed, explored and compared with the purpose of extracting dynamical information on these well characterized "model" protein systems.
© (1989) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Joel M. Friedman, Joel M. Friedman, M. R. Ondrias, M. R. Ondrias, } "Fast Structural Relaxations In Hemoglobin And Myoglobin: An Analysis Of Time Resolved Raman Studies", Proc. SPIE 1055, Raman Scattering, Luminescence and Spectroscopic Instrumentation in Technology, (5 July 1989); doi: 10.1117/12.951591; https://doi.org/10.1117/12.951591
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