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 flash photolysis together with near ultraviolet, visible, and near and mid-infrared spectroscopies over wide ranges in time (50ns-10ks), temperature (60-320K), and pressure (0.1-100MPa). Pressure is used both as a static thermodynamic variable and as a perturbation to study protein motions. 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 together with high pressure and low temperature. 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 novel information on the glass-like behavior of proteins, including the slaved glass transition and glass-like relaxation processes near the transition temperature. We also extend our studies to more complicated proteins such as horseradish peroxidase and cytochrome.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 26, 1989
- Accession Number
- ADA206503
Entities
People
- Hans Frauenfelder
- Robert D. Young
Organizations
- University of Illinois Urbana–Champaign