Read about the science being performed at Brown University's Structural Biology Core Facility.
Koveal D, Clarkson MW, Wood TK, Page R, and Peti W. "Ligand Binding Reduces Conformational Flexibility in the Active Site of Tyrosine Phosphatase Related to Biofilm Formation A (TpbA) from Pseudomonas aeruginosa" Journal of Molecular Biology 2013 (Advance publication)
Brown University graduate student Dorothy Koveal, from the Page-Peti lab, used NMR spectroscopy to determine the structure of a phosphatase that controls biofilm formation in P. aeruginosa in isolation and in complex with phosphate. Using the 500 MHz NMR spectrometer at Brown University, she also obtained information about the dynamics of the protein's backbone amide groups. These experiments showed that the unbound protein had significantly greater flexibility in its active site than the phosphate-bound protein. This restraint of motion may be related to enzymatic activity or substrate specificity.
Koveal D, Schuh-Nuhfer N, Ritt D, Page R, Morrison DK, and Peti W. "A CC-SAM, for Coiled-Coil Sterile-α Motif, Domain Targets the Scaffold KSR-1 to Specific Sites in the Plasma Membrane" Science Signaling 2012, 5 (255): ra94.
Brown University graduate student Dorothy Koveal, from the Page-Peti lab, used NMR spectroscopy to determine the structure of a novel domain fusing a coiled-coil motif to a sterile-α motif. With the assistance of collaborators at the National Cancer Institute, she found that this domain targeted the scaffolding protein KSR-1 to membrane ruffles in vivo. Using the Brown University 500, she determined that CC-SAM underwent a structural rearrangement in the presence of specific kinds of lipid micelles and bicelles that explained the domain's targeting capabilities.