Automated Assignment of Backbone Resonances Using Residual Dipolar Couplings Acquired from a Protein with Known Structure
This method reduces the financial cost and time for protein structure determination by automating resonance assignment, which is beneficial for validating solution state structures in structural biology.
The researchers tackled the problem of backbone resonance assignment in NMR spectroscopy by developing a method that uses only residual dipolar coupling (RDC) data, enabling simultaneous order tensor estimation and assignment, and demonstrated its viability with simulated data from protein domain 1A1Z.
Resonance assignment is a critical first step in the investigation of protein structures using NMR spectroscopy. The development of assignment methods that require less experimental data is possible with prior knowledge of the macromolecular structure. Automated methods of performing the task of resonance assignment can significantly reduce the financial cost and time requirement for protein structure determination. Such methods can also be beneficial in validating a protein's solution state structure. Here we present a new approach to the assignment problem. Our approach uses only RDC data to assign backbone resonances. It provides simultaneous order tensor estimation and assignment. Our approach compares independent order tensor estimates to determine when the correct order tensor has been found. We demonstrate the algorithm's viability using simulated data from the protein domain 1A1Z.