Trapping a transition state in a computationally designed protein bottle
Abstract
The transition state of a chemical transformation is inherently fleeting because the structure is high in energy. Nonetheless, Pearson et al. trapped a classical example of a bond rotation transition state using a modified protein (see the Perspective by Romney and Miller). The biphenyl molecule passes through an energy maximum when its rings rotate through a parallel position. A pocket within the editing domain of threonyl–transfer RNA synthetase was modified to stabilize parallel biphenyl rings, allowing further characterization of this normally transient structure.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Feb 20, 2015
- Source ID
- 10.1126/science.aaa2424
Entities
People
- Aaron D. Pearson
- David Baker
- Fariborz Nasertorabi
- Gye Won Han
- Jeremy H. Mills
- Peter G. Schultz
- Raymond C. Stevens
- Yifan Song
Organizations
- Defense Threat Reduction Agency
- National Institutes of Health
- University of Southern California
- University of Washington
- Yusuf Hamied Department of Chemistry