2012年12月5日，中科院武汉与数学研究所研究员唐淳博士应邀访问研究所并举办学术讲座。

2012年12月5日，中科院武汉与数学研究所研究员唐淳博士应邀访问研究所并举办学术讲座。讲座的题目为：Direct Visualization of Protein Dynamics Using PRE NMR。朱冰博士主持讲座。

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.