A Measurement of the Proton Structure Function g2p at Low Q2

Experiments at Jefferson Lab have been conducted to extract the nucleon spin-dependent structure functions over a wide kinematic range. Higher moments of these quantities provide tests of QCD sum rules and predictions of chiral perturbation theory ($\chi$PT). While precise measurements of $g_{1}^n$, $g_{2}^n$, and $g_1^p$ have been extensively performed, the data of $g_2^p$ remain scarce. Discrepancies were found between existing data related to $g_2$ and theoretical predictions. Results on the proton at large $Q^2$ show a significant deviation from the Burkhardt-Cottingham sum rule, while results for the neutron generally follow this sum rule. The next-to-leading order $\chi$PT calculations exhibit discrepancy with data on the longitudinal-transverse polarizability $\delta_{LT}^n$. Further measurements of the proton spin structure function $g_2^p$ are desired to understand these discrepancies.

Experiment E08-027 (g2p) was conducted at Jefferson Lab in experimental Hall A in 2012. Inclusive measurements were performed with polarized electron beam and a polarized ammonia target to obtain the proton spin-dependent structure function $g_2^p$ at low Q$^2$ region (0.02$<$Q$^2$$<$0.2 GeV$^2$) for the first time. The results can be used to test the Burkhardt-Cottingham sum rule, and also allow us to extract the longitudinal-transverse spin polarizability of the proton, which will provide a benchmark test of $\chi$PT calculations. This thesis will present and discuss the very preliminary results of the transverse asymmetry and the spin-dependent structure functions $g_1^p$ and $g_2^p$ from the data analysis of the g2p experiment .

Development and Application of Covalent-Labeling Strategies for the Large-Scale Thermodynamic Analysis of Protein Folding and Ligand Binding

Thermodynamic stability measurements on proteins and protein-ligand complexes can offer insights not only into the fundamental properties of protein folding reactions and protein functions, but also into the development of protein-directed therapeutic agents to combat disease. Conventional calorimetric or spectroscopic approaches for measuring protein stability typically require large amounts of purified protein. This requirement has precluded their use in proteomic applications. Stability of Proteins from Rates of Oxidation (SPROX) is a recently developed mass spectrometry-based approach for proteome-wide thermodynamic stability analysis. Since the proteomic coverage of SPROX is fundamentally limited by the detection of methionine-containing peptides, the use of tryptophan-containing peptides was investigated in this dissertation. A new SPROX-like protocol was developed that measured protein folding free energies using the denaturant dependence of the rate at which globally protected tryptophan and methionine residues are modified with dimethyl (2-hydroxyl-5-nitrobenzyl) sulfonium bromide and hydrogen peroxide, respectively. This so-called Hybrid protocol was applied to proteins in yeast and MCF-7 cell lysates and achieved a ~50% increase in proteomic coverage compared to probing only methionine-containing peptides. Subsequently, the Hybrid protocol was successfully utilized to identify and quantify both known and novel protein-ligand interactions in cell lysates. The ligands under study included the well-known Hsp90 inhibitor geldanamycin and the less well-understood omeprazole sulfide that inhibits liver-stage malaria. In addition to protein-small molecule interactions, protein-protein interactions involving Puf6 were investigated using the SPROX technique in comparative thermodynamic analyses performed on wild-type and Puf6-deletion yeast strains. A total of 39 proteins were detected as Puf6 targets and 36 of these targets were previously unknown to interact with Puf6. Finally, to facilitate the SPROX/Hybrid data analysis process and minimize human errors, a Bayesian algorithm was developed for transition midpoint assignment. In summary, the work in this dissertation expanded the scope of SPROX and evaluated the use of SPROX/Hybrid protocols for characterizing protein-ligand interactions in complex biological mixtures.