Share Email Print

Proceedings Paper

Fast Structural Relaxations In Hemoglobin And Myoglobin: An Analysis Of Time Resolved Raman Studies
Author(s): Joel M. Friedman; M. R. Ondrias
Format Member Price Non-Member Price
PDF $17.00 $21.00

Paper 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.

Paper Details

Date Published: 5 July 1989
PDF: 8 pages
Proc. SPIE 1055, Raman Scattering, Luminescence and Spectroscopic Instrumentation in Technology, (5 July 1989); doi: 10.1117/12.951591
Show Author Affiliations
Joel M. Friedman, AT&T Bell Laboratories (United States)
M. R. Ondrias, University of New Mexico (United States)

Published in SPIE Proceedings Vol. 1055:
Raman Scattering, Luminescence and Spectroscopic Instrumentation in Technology
Fran Adar; James E. Griffiths; Jeremy M. Lerner, Editor(s)

© SPIE. Terms of Use
Back to Top
Sign in to read the full article
Create a free SPIE account to get access to
premium articles and original research
Forgot your username?