Welcome to the Carter Lab

 
 

The Carter lab at UNC Chapel Hill uses structural biology, bioinformatic, molecular genetic, and biophysical techniques to deepen understanding of the mechanistic basis and historical origins of enzyme catalysis. One of the challenging questions we study is how the chemical free energy released by NTP hydrolysis is converted into protein conformational changes. This video shows a wooden time-keeping device, which is a metaphor for a new allosteric coupling mechanism that converts domain movement into rate acceleration of amino acid activation by Tryptophanyl-tRNA synthetase. The rotating triangle in the center of the device functions similarly to the active-site Mg2+ ion; it senses the domain configuration and contributes to the rate acceleration according to the relative position of the two domains, which in this metaphor are represented by the oscillating bar.

Video courtesy of Piers Samwell-Smith