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 (60-300 K), time (50ns-lks), and, most importantly for this grant, pressure (0.1-200MPA). A simple biomolecular reaction - carbon monoxide binding to myoglobin is studied. Previous work over wide ranges in temperature and time has been crucial to developing models of protein dynamics. Pressure effects are less well explored. Studies over wide ranges of both temperature and pressure can probe protein states which are not accessible by varying only temperature or pressure. A hierarchical model of protein dynamics was developed 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: myoglobin.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 28, 1987
- Accession Number
- ADA177825
Entities
People
- Hans Frauenfelder
- Robert D. Young
Organizations
- University of Illinois Urbana–Champaign