Fast Structural Relaxations in Hemoglobin and Myoglobin

An Analysis of Time Resolved Raman Studies

Joel M. Friedman, M. R. Ondrias

Research output: Contribution to journalArticle

2 Citations (Scopus)

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 studiesstudies to date have been theoretical endeavors utilizing molecular dynamics simulations. Unfortunately comparable experiments thatthat 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.

Original languageEnglish (US)
Pages (from-to)216-223
Number of pages8
JournalProceedings of SPIE - The International Society for Optical Engineering
Volume1055
DOIs
StatePublished - Jul 5 1989
Externally publishedYes

Fingerprint

Structural relaxation
myoglobin
Hemoglobin
Myoglobin
hemoglobin
Raman
Hemoglobins
proteins
Proteins
Protein
Biophysics
biophysics
Global Dynamics
Reactivity
Molecular Dynamics Simulation
Molecular dynamics
reactivity
molecular dynamics
Motion
Computer simulation

ASJC Scopus subject areas

  • Applied Mathematics
  • Electronic, Optical and Magnetic Materials
  • Condensed Matter Physics
  • Electrical and Electronic Engineering
  • Computer Science Applications

Cite this

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