Controlling Protein Conformations to Explore Unprecedented Material Properties by Single-Molecule Surgery
Abstract
The primary objective of our single-molecule material science project is to mechanically and optically control and regulate single-molecule protein conformations to explore unprecedented properties and capture such exclusive states in real-time at an extreme molecular sensitivity. Bring up never-detected and novel properties from proteins, over the last year, we have (1) revealed a time bunching effect of protein conformational motions under enzymatic reactions, which suggests that new material properties can be selectively induced and intensified under specific conditions identified by single-molecule experiments. The unprecedented properties can only be observed and studied by our single-molecule approaches; (2) discovered, for the first time, oscillatory enzyme conformational motions that are critical for the enzyme activity, which shed light on developing new material technology to induce, intensify, and lock random and transient material properties; (3) demonstrated a manipulation of protein conformations by force pulling a specific residue of a target protein, achieving a new technical milestone towards our goal of manipulating single-molecule proteins to create new material properties; (4) explore matrix magnetic tweezers manipulation of protein activities in enzymatic reaction and protein sensing; and (5) identified a generally existed, but hidden for conventional measurements, time bunching effect of protein conformational motions under enzymatic reactions.
Document Details
- Document Type
- Technical Report
- Publication Date
- Aug 17, 2012
- Accession Number
- ADA584676
Entities
People
- Hong P. Lu
Organizations
- Bowling Green State University