Citizen science projects can be used in college laboratory settings to allow students to gain hands-on experience in research during emergency remote learning. During the 2020 spring semester, we used the citizen science project, Budburst, in our introductory biology laboratory during the COVID-19-induced emergency remote learning period. The instructors were able to quickly adapt the project for emergency remote teaching because of the versatility of citizen science projects. The goals of this paper are to describe the project the students completed and to determine which data literacy and scientific writing skills were gained through the process. The students were provided with the research question: "How does temperature affect the phenophases of your trees?" Students collected their own data and downloaded Budburst data sets from the website to compare between years and to connect their results to long-term temperature data sets. The final project was a scientific paper based on their findings from both data sets. After the semester, a subset of papers was scored by two researchers using a previously validated rubric designed to evaluate students' research skills. We evaluated students' higher-order thinking by investigating their ability to develop a prediction statement, and to improve their qualitative skills by developing graphs, statements on the limitations for methods and results, and alternative explanations for their findings. We saw that using citizen science during remote teaching enabled the students to gain authentic research experiences and continue to improve their skill set even if they could not be in the laboratory.
The pKa values of ionizable groups in proteins report the free energy of site-specific proton binding and provide a direct means of studying pH-dependent stability. We measured histidine pKa values (H3, H22, and H105) in the unfolded (U), intermediate (I), and sulfate-bound folded (F) states of RNase P protein, using an efficient and accurate nuclear magnetic resonance-monitored titration approach that utilizes internal reference compounds and a parametric fitting method. The three histidines in the sulfate-bound folded protein have pKa values depressed by 0.21 ± 0.01, 0.49 ± 0.01, and 1.00 ± 0.01 units, respectively, relative to that of the model compound N-acetyl-L-histidine methylamide. In the unliganded and unfolded protein, the pKa values are depressed relative to that of the model compound by 0.73 ± 0.02, 0.45 ± 0.02, and 0.68 ± 0.02 units, respectively. Above pH 5.5, H22 displays a separate resonance, which we have assigned to I, whose apparent pKa value is depressed by 1.03 ± 0.25 units, which is ~0.5 units more than in either U or F. The depressed pKa values we observe are consistent with repulsive interactions between protonated histidine side chains and the net positive charge of the protein. However, the pKa differences between F and U are small for all three histidines, and they have little ionic strength dependence in F. Taken together, these observations suggest that unfavorable electrostatics alone do not account for the fact that RNase P protein is intrinsically unfolded in the absence of ligand. Multiple factors encoded in the P protein sequence account for its IUP property, which may play an important role in its function.
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