Pressure Studies of Protein Dynamics.
Abstract
The relation between dynamic structure and function of proteins is investigated. Protein dynamics are studied by observing the phenomena induced by flash photolysis using near ultraviolet, optical, and infrared spectroscopies over wide ranges in temperature (60-300K), time (50ns-Iks), and, pressure (0.1-200MPa). Initially we study a simple biomolecular reaction - carbon monoxide binding to myoglobin. Previous work over wide ranges in temperature and time has been crucial to developing models of protein dynamics. We developed a hierarchical model of protein dynamics which promises to contribute to understanding both biomolecular reactions and the physics of amorphous solids and glasses. The combined pressure and temperature experiments will test various features of the hierarchical model including the glass-like properties of proteins. Keywords: Proteinquake, flash photolysis, spectroscopic markers, ligand binding.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 20, 1987
- Accession Number
- ADA179028
Entities
People
- Hans Frauenfelder
- Robert D. Young
Organizations
- University of Illinois Urbana–Champaign