3D solution structure of the E73 protein.

To understand the molecular links between protein chemical structures, internal dynamics, and biochemical functions, we focus on the questions: What is the connection between a protein's biological function and its structural dynamics (i.e. the flexibility of various structural elements within a protein's three-dimensional structure)? How do atomic structures and internal dynamics modulate biochemical activity? What is the functional significance of evolutionary conservation of certain amino acid residues in protein families? Proteins of interest involve (1) crenarchaeal viral proteins from Sulfolobus spindle shaped viruses; (2) proteins involved in heme acquisition and Staphylococcus aureus pathogen growth and survival; (3) leaf senescence and nitrogen remobilization in plants; (4) protein dynamics studies of functionally altered mutants of the tryptophan repressor protein (TrpR). 
The adjacent figure shows the 3D solution structure of the E73 protein from the hyperthermophilic crenarchaeal Sulfolobus Spindle Shaped Virus – Ragged Hills (SSV-RH) as determined by NMR.



Spectroscopy, Protein Chemistry, NMR, Chemical Biology, Biophysical, Biochemistry