Kristine Maxwell

Kristine Maxwell is a rising senior at Truman State University. She is currently majoring. in Chemistry and intends to specialize in environmental chemistry after she obtains her Bachelor of Science in Chemistry. A little insight into her personal life: she grew up in St. Louis, Missouri, and hopes to have enough money so that she can travel the world comfortably. She has fou siblings and her favorite color is sky blue. This summer 2022, Kristine is working with Brandi James in Dr. Anna Gudmundsdottir's lab to study the photodynamic motions of organic azide crystals, specifically of 1-azido-2-nitrobenzene (1A-2NB) crystals. Dynamic azide crystals are materials that respond to external stimuli, release N2 gas, and have the ability to convert light to mechanical motion such as bending, flipping, cracking, etc. When these crystals are paired with low-energy visible light, we can influence cost-effective and sustainable reactions since we are minimizing solvent waste. However, before we can use these azide crystals in applications such as robotics, sensors, etc., we need to understand their crystal packing and forces between the lattices, which dictate how the crystal will react to external stimuli. Throughout the summer, she will continue to learn several complex laboratory techniques involving such as synthesis, characterization of compounds (TLC, IR, NMR spectroscopy), photolysis methods (including sample preparation), crystallization methods, and waste safety whilst handling these materials. Overall, because azides are potentially explosive, we take a lot of safety measures into our procedures and follow them meticulously.

Rahel Lema

Rahel Lema is a rising sophomore at the University of Maryland, Baltimore County, where she studies Biochemistry and Molecular Biology. She plans on pursuing her Ph.D. in chemistry or biochemistry after completing her undergraduate studies. This summer, she is working in Dr. James Mack’s lab under the guidance of graduate student Jazmine Crain, investigating proteins’ biochemical responses under mechanochemical conditions. Mechanical stress in proteins has gained significant research attention in that prolonged, destabilizing mechanical energy has been identified as a potential factor in the progression of selective neurodegenerative diseases, such as Alzheimer's and Parkinson’s Disease. Researchers have been trying to understand the molecular events of protein unfolding and destabilization via mechanical stress but lack the appropriate tools to do so. Therefore, more information about the response of proteins to mechanical stress is required. We look to employ mechanochemistry as a tool to test the events of protein unfolding. With this, we can directly apply mechanical stress to proteins and track their physiological and structural changes. By using a temperature and oscillation frequency controlled milling system, we are able to observe the degree of energy in which transforms the rheology and function of the protein. To test our method of various mechanical conditions, we choose to work with the model protein BSA (bovine serum albumin). BSA is a protein that is found in plasma and serum, which maintains the pressure and flow of body compartments, as well as several other capabilities. To subject the protein to stress, it is placed along with a 3”16” stainless steel ball at a range of oscillation frequencies in a ball mill. Techniques such as MALDI-MS TOF allow for the detection of structural changes after milling. To measure functional changes, molecular interactions between BSA and the drug warfarin are analyzed through Isothermal Titration Calorimetry (ITC).

Nikki Krahulik

Nikki Krahulik is a rising senior at Grove City College. She is pursuing a chemistry degree with a focus on synthetic chemistry. She is from Lancaster, Pennsylvania. This summer, Nikki is conducting research under Dr. Wei Liu with Chao Wang as her graduate student mentor. She is investigating the synthesis of RAE—redox-active esters—via in situ reactions. RAEs are reactive and can undergo either reductive or oxidative quenching, which then allows for further reactions that can add a trifluoromethylated group to an alkyl molecule through copper-catalyzed decarboxylative trifluoromethylation. The importance of the synthesis of such products is that trifluoromethylated groups have grown in popularity in the medicinal chemistry field. The C-F bond is a strong bond that gives metabolic stability and increases lipophilicity that is important for transportation through the lipophilic membrane. This research investigates the ability and methods necessary to add a trifluoromethylated group to an alkyl group.