Influence of Hydration and Protein Collective Motions on Biological activities
Abstract
The understanding of conformational changes or dynamics of proteins will shed light on the physics,functions of biological machinery (molecular self-assembly), and biological energy transport. Specifically,biological functions of proteins in aqueous environments, such as enzymatic activity, oxygen transport, neuron signal transmission, and ion channels for signaling currents, depend on structural changes, flexibility, and protein-water interface. It has been suggested that low-frequency collective vibrational modes (<3 THz) involving dynamical networks extending throughout the protein play a crucial role in controlling the structural changes. As a general rule, biological functions of proteins occur in aqueous environments. While solvation effects on proteins play an essential role in the structure, stability, and dynamics of proteins, our understanding of solvent dynamics at the protein-water interface remains inadequate. The most straightforward approach to monitoring the low-frequency collective vibrational motions of proteins in aqueous environments and the interfacial dynamics is their direct detection via megahertz-to-terahertz spectroscopy. In response, we have built a unique terahertz frequency-domain system with highest precision, highest sensitivity and largest continuous-frequency range to study solvent effectsthat drive hydrophobic/hydrophilic interactions and picosecond internal motions of solvated proteins. The frequency range of the system spans more than five orders of magnitude from 10 MHz to 3 THz. Systems examined in this project include an aqueous-stable enzyme (lysozyme), neuron tau proteins, and hemeproteins (myoglobin, cytochrome_c).
Document Details
- Document Type
- DoD Grant Award
- Publication Date
- Jul 11, 2018
- Source ID
- FA95501810263
Entities
People
- Vinh Nguyen
Organizations
- Air Force Office of Scientific Research
- United States Air Force
- Virginia Tech