2012年12月5日，中科院武漢與數(shù)學研究所研究員唐淳博士應邀訪問研究所并舉辦學術(shù)講座。講座的題目為：Direct Visualization of Protein Dynamics Using PRE NMR。朱冰博士主持講座。

Abstract:

Mounting experimental evidences and theoretical calculations have shown that at ambient temperature, a protein fluctuates among different conformations[1], thus enabling the protein to execute its function. The lowest-energy conformation is termed ground-state structure; conformations with higher energies and lower populations are termed transient structures. Transient structures refer to either transient conformational change of a single polypeptide or transient formation of protein-protein complexes. My group is actively developing novel paramagnetic NMR methods to directly visualize protein transient structures and protein dynamics[2].

Most biomolecular NMR studies focus on diamagnetic samples, as the presence of paramagnetic species expedites nuclear relaxation and deteriorates NMR spectrum. Nevertheless, deliberate introduction of a paramagnetic probe at desired site in a protein offers a plethora of information. Inverse proportional to the sixth power of the distance between a paramagnetic probe and a nucleus, paramagnetic relaxation enhancement (PRE) is exquisitely sensitive to lowly populated transient structures. In this presentation, I will talk about 1) principle of PRE NMR to visualize protein dynamics, 2) our efforts to rigidify the paramagnetic probe, 3) spatial and temporal characterization of protein dynamics using differentially scaled PRE, and 4) applications of PRE NMR.

Abstract:

Mounting experimental evidences and theoretical calculations have shown that at ambient temperature, a protein fluctuates among different conformations[1], thus enabling the protein to execute its function. The lowest-energy conformation is termed ground-state structure; conformations with higher energies and lower populations are termed transient structures. Transient structures refer to either transient conformational change of a single polypeptide or transient formation of protein-protein complexes. My group is actively developing novel paramagnetic NMR methods to directly visualize protein transient structures and protein dynamics[2].

Most biomolecular NMR studies focus on diamagnetic samples, as the presence of paramagnetic species expedites nuclear relaxation and deteriorates NMR spectrum. Nevertheless, deliberate introduction of a paramagnetic probe at desired site in a protein offers a plethora of information. Inverse proportional to the sixth power of the distance between a paramagnetic probe and a nucleus, paramagnetic relaxation enhancement (PRE) is exquisitely sensitive to lowly populated transient structures. In this presentation, I will talk about 1) principle of PRE NMR to visualize protein dynamics, 2) our efforts to rigidify the paramagnetic probe, 3) spatial and temporal characterization of protein dynamics using differentially scaled PRE, and 4) applications of PRE NMR.