Pressure Studies of Protein Dynamics.

Abstract

In this research we extend and deepen our studies of the relation between dynamic structure and function in proteins. We study protein dynamics using flesh photolysis together with near ultraviolet, visible, and near and mid-infrared spectroscopies over wide ranges in time (50 ns-10 ks), temperature (60-320K), and pressure (0.1-100 MPa). Initially we study a simple biomolecular reaction -- carbon monoxide (CO) binding to myoglobin (Mb). We have greatly expanded knowledge of pressure effects on proteins by using the infrared CO stretching frequencies in MbCO as a probe. The combined pressure and temperature studies shed new light on various features of the hierarchical model of protein substates and motions. These studies also provide much information on the glass like behavior of proteins, including the slaved glass transition and glass-like relaxation processes near the transition temperature. Keywords: Protein dynamics, Pressure, Myoglobin, Hierarchy of substates, Flash photolysis, Carbon dioxide(CO) stretching bands, Glass like properties.

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Document Details

Document Type
Technical Report
Publication Date
Feb 26, 1988
Accession Number
ADA192386

Entities

People

  • Hans Frauenfelder
  • Robert D. Young

Organizations

  • University of Illinois Urbana–Champaign

Tags

DTIC Thesaurus Topics

  • Biochemistry
  • Biological Sciences
  • Biophysics
  • Carbon Monoxide
  • Chemical Engineering
  • Chemistry
  • Classification
  • Dielectric Gases
  • Dynamics
  • Ecology
  • Frequency
  • Glass Transition Temperature
  • Hierarchies
  • Military Research
  • Molecular Biology
  • Physics
  • Spectra

Readers

  • Mechanical Engineering/Mechanics of Materials.
  • Molecular and Cellular Biochemistry
  • Spectroscopy.