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Klewe, C; Emori, S; Li, Q; Yang, M; Gray, B A; Jeon, H-M; Howe, B M; Suzuki, Y; Qiu, Z Q; Shafer, P; et al(
, New Journal of Physics)
Abstract We present the first theoretical and experimental evidence of time-resolved dynamic x-ray magnetic linear dichroism (XMLD) measurements of GHz magnetic precessions driven by ferromagnetic resonance in both metallic and insulating thin films. Our findings show a dynamic XMLD in both ferromagnetic Ni 80 Fe 20 and ferrimagnetic Ni 0.65 Zn 0.35 Al 0.8 Fe 1.2 O 4 for different measurement geometries and linear polarizations. A detailed analysis of the observed signals reveals the importance of separating different harmonic components in the dynamic signal in order to identify the XMLD response without the influence of competing contributions. In particular, RFmore »magnetic resonance elicits a large dynamic XMLD response at the fundamental frequency under experimental geometries with oblique x-ray polarization. The geometric range and experimental sensitivity can be improved by isolating the 2 ω Fourier component of the dynamic response. These results illustrate the potential of dynamic XMLD and represent a milestone accomplishment toward the study of GHz spin dynamics in systems beyond ferromagnetic order.« less
Free, publicly-accessible full text available January 1, 2023
Enzyme encapsulation in metal-organic frameworks (MOFs)/covalent-organic frameworks (COFs) provides advancement in biocatalysis, yet the structural basis underlying the catalytic performance is challenging to probe. Here, we present an effective protocol to determine the orientation and dynamics of enzymes in MOFs/COFs using site-directed spin labeling and electron paramagnetic resonance spectroscopy. The protocol is demonstrated using lysozyme and can be generalized to other enzymes.
Free, publicly-accessible full text available September 17, 2022
With the rapid growth of online learning at community colleges and the low course completion and performance associated with it, there has been increasing need to identify effective ways to address the challenges in online teaching and learning at this particular setting. Based on open-ended survey responses from 105 instructors and 365 students from multiple community colleges in a state, this study examined instructors’ and students’ perceptions of effective and ineffective instructional practices and changes needed in online coursework. By combining structural topic modelling techniques with human coding, we identified instructional practices that were perceived by both instructors and studentsmore »as effective in supporting online learning as well as ineffective and needing improvement. Moreover, we identified a handful of misalignments between instructors and students in their perceptions of online teaching, including course workload and effective ways to communicate.« less
Free, publicly-accessible full text available July 1, 2022
Multiple-enzyme cooperation simultaneously is an effective approach to biomass conversion and biodegradation. The challenge, however, lies in the interference of the involved enzymes with each other, especially when a protease is needed, and thus, the difficulty in reusing the enzymes; while extracting/synthesizing new enzymes costs energy and negative impact on the environment. Here, we present a unique approach to immobilize multiple enzymes, including a protease, on a metal–organic material (MOM) via co-precipitation in order to enhance the reusability and sustainability. We prove our strategy on the degradation of starch-containing polysaccharides (require two enzymes to degrade) and food proteins (require amore »protease to digest) before the quantification of total dietary fiber. As compared to the widely adopted “official” method, which requires the sequential addition of three enzymes under different conditions (pH/temperature), the three enzymes can be simultaneously immobilized on the surface of our MOM crystals to allow for contact with the large substrates (starch), while MOMs offer sufficient protection to the enzymes so that the reusability and long-term storage are improved. Furthermore, the same biodegradation can be carried out without adjusting the reaction condition, further reducing the reaction time. Remarkably, the simultaneous presence of all enzymes enhances the reaction efficiency by a factor of ∼3 as compared to the official method. To our best knowledge, this is the first experimental demonstration of using aqueous-phase co-precipitation to immobilize multiple enzymes for large-substrate biocatalysis. The significantly enhanced efficiency can potentially impact the food industry by reducing the labor requirement and enhancing enzyme cost efficiency, leading to reduced food cost. The reduced energy cost of extracting enzymes and adjusting reaction conditions minimize the negative impact on the environment. The strategy to prevent protease damage in a multi-enzyme system can be adapted to other biocatalytic reactions involving proteases.« less
Free, publicly-accessible full text available September 3, 2022
An extensive theoretical and empirical literature stresses the challenges of online learning, especially among students enrolled in open-access institutions who often struggle more due to job and family commitments and a lack of self-regulated learning skills. As online expansion continues in higher education, understanding the specific challenges students encounter in online coursework, and learning strategies that can help them cope with these challenges, can provide valuable insights to be widely shared. Using open-ended survey data collected from 365 students at a state community college system, this study examined students’ perceptions of challenges of online learning that may lead to undesirablemore »learning outcomes and specific strategies they found effective in addressing these challenges. We combined structural topic modeling and human coding in analyzing student responses. Three sets of challenges—including insufficient time management skills, greater tendencies of multitasking and being distracted in an online learning environment, and ineffective interaction and frustrations with help-seeking—emerged from student responses. In response to these challenges, students reflected on ways to improve online learning experiences and outcomes, including improving time management skills, maintaining an organized and distraction-free study environment, proactively seeking help, and using study strategies to improve learning effectiveness.« less
Free, publicly-accessible full text available June 8, 2022
Site-directed spin labeling (SDSL) in combination with electron paramagnetic resonance (EPR) spectroscopy probes the otherwise inaccessible structural information in complex biological systems. We recently extended SDSL-EPR to reveal the relative orientation and backbone dynamics of enzymes upon encapsulation in mesoporous nanostructures, which set the structural basis underlying the observed biocatalytic activity. Our strategy had generated interest in the biocatalysis community, and thus in this resource article, we contribute an introduction to the principles and experimental procedure that generalize SDSL-EPR to heterogeneous biocatalysis. We will focus on enzymes in mesoporous materials with examples demonstrating the methods and cautions of potential pitfalls.more »The ultimate goal is to provide the biocatalysis community with a powerful resource to fill in a long-standing knowledge gap in heterogeneous biocatalysis and the structure-function relationship of enzymes at the interface of enzyme-mesoporous materials and utilize the structural insights to guide the rational design of porous platforms for enzyme immobilization.« less
Co-precipitation of enzymes in metal-organic frameworks is a unique enzyme-immobilization strategy but is challenged by weak acid-base stability. To overcome this drawback, we discovered that Ca2+ can co-precipitate with carboxylate ligands and enzymes under ambient aqueous conditions and form enzyme@metal-organic material composites stable under a wide range of pHs (3.7–9.5). We proved this strategy on four enzymes with varied isoelectric points, molecular weights, and substrate sizes—lysozyme, lipase, glucose oxidase (GOx), and horseradish peroxidase (HRP)—as well as the cluster of HRP and GOx. Interestingly, the catalytic efficiency of the studied enzymes was found to depend on the ligand, probing the originsmore »of which resulted in a correlation among enzyme backbone dynamics, ligand selection, and catalytic efficiency. Our approach resolved the long-lasting stability issue of aqueous-phase co-precipitation and can be generalized to biocatalysis with other enzymes to benefit both research and industry.« less
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