Musical Expertise and Melodic Structure in Memory for Musical Notation

Two experiments plus a pilot investigated the role of melodic structure on short-term memory for musical notation by musicians and nonmusicians. In the pilot experiment, visually similar melodies that had been rated as either "good" or "bad" were presented briefly, followed by a 15-sec retention interval and then recall. Musicians remembered good melodies better than they remembered bad ones: nonmusicians did not distinguish between them. In the second experiment, good, bad, and random melodies were briefly presented, followed by immediate recall. The advantage of musicians over nonmusicians decreased as the melody type progressed from good to bad to random. In the third experiment, musicians and nonmusicians divided the stimulus melodies into groups. For each melody, the consistency of grouping was correlated with memory performance in the first two experiments. Evidence was found for use of musical groupings by musicians and for use of a simple visual strategy by nonmusicians. The nature of these musical groupings and how they may be learned are considered. The relation of this work to other studies of comprehension of symbolic diagrams is also discussed.

Structure-Function Relations in the PI-PLC/GDPD Enzyme Superfamily

Phosphatidylinositol-specific phospholipases C (PI-PLC) are known to participate in many eukaryotic signal transduction pathways and act as virulence factors in lower organisms. Glycerophosphoryl diester phosphodiesterase (GDPD) enzymes are involved in phosphate homeostasis and phospholipid catabolism for energy production. Streptomyces antibioticus phosphatidylinositol-specific phospholipase C (SaPLC1) is a 38 kDa enzyme that displays characteristics of both enzyme superfamilies, representing an evolutionary link between these divergent enzyme classes. SaPLC1 also boasts a unique catalytic mechanism that involves a trans 1,6-cyclic inositol phosphate intermediate instead of the typical cis 1,2-cyclic inositol phosphate. The mechanism by which this occurs is still unclear. To attack this problem, we established a wide mutagenesis scan of the active site and measured activities of alanine mutants. A chemical rescue assay was developed to verify that the activity loss was due to the removal of the functional role of the mutated residue. 31P-NMR was employed in characterizing and quantifying intermediates in mutants that slowed the reaction sufficiently. We found that the H37A and H76A mutations support the hypothesis that these structurally conserved residues are also conserved in terms of their catalytic roles. H37 was found to be the general base (GB), while H76 plays the role of general acid (GA). K131 was identified as a semi-conserved key positive charge donor found at the entrance of the active site. By elucidating the SaPLC1 mechanism in relation to its active site architecture, we have increased our understanding of the structure-function relations that support catalysis in the PI-PLC/GDPD superfamily. These findings provide groundwork for in vivo studies of SaPLC1 function and its possible role in novel signaling or metabolism in Streptomyces.