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Research was conducted to examine a ligand-binding protein (SIS2) of a glutamate receptor ion channel (GluR) via solution scattering studies to investigate GluR-binding and signal-transduction mechanisms. The solution scattering properties of the free and agonist-bound states of a ligand-binding domain of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor subunit GluRD were compared. Results indicate a molecular envelope for the construct in solution.

Research was conducted to examine the properties of a mutant hexokinase I, in which residues critical to the stability of the dimer have been changed by directed mutation. The resulting mutant was shown to exist in solution as a monomer at elevated concentrations of enzyme, either in the presence or absence of ligands. Results indicate that the allosteric regulation of catalysis in monomeric hexokinase I probably involves an interface between the N- and C-terminal halves, similar to ones defined by crystal structures.

The quaternary structure of the V1 ATPase from the tobacco hornworm Manduca sexta and the F1 ATPase from Escherichia coli was characterized using small-angle X-ray scattering. The radii of gyration of the V1 and F1 complexes as well as the shape of the V1 ATPase were also determined. Experimental results showed that a seventh mass, which is thought to be the stalk that links V1 with the membrane domain V0 in the intact V1V0-ATPase, extends perpendicularly to the center of the hexameric unit.

A study was conducted to analyze the quarternary structures of the thiamine diphosphate dependent enzyme pyruvate decarboxylase from Saccharomyces cerevisiae, Zymomonas mobilis and Pisum sativuum. X-ray solution scattering was carried out to perform the analysis while solutions were prepared from enzyme stock solutions. Results indicated that mutant E51 is a critical component in cofactor binding and catalytic activity.

Magnesium ions initiate the formation of the catalytically active dimer and the activity of enzyme I from the phosphoenolpyruvate system of Staphylococcus carnosus. X-ray scattering patterns of the enzyme reveals an increase in the radius of gyration and the molecular mass in the presence of Mg2+ and the substrate, phosphoenolpyruvate. The substrate appears to shift the equilibrium towards the formation of the active dimer by reducing the rate of dissociation of the phophorylated dimer.

The pH dependence of the three-dimensional quarternary structure of yeast pyruvate decarboxylase (PDC) was examined in the pH range from 6.2 to 8.4 by a synchroton radiation solution x-ray scattering study. The equilibrium between tetramers and dimers occurs at about pH 7.5 and the PDC's catalytic activity is dependent on the volume fraction of tetramer. The experimental observations of an equilibrium shift and formation of octamers were further analyzed. These observations were found to indicate that the dimers must undergo a conformational change when forming the tetramer, as suggested by earlier studies.