Bioethics is an important aspect of the core competency of biology of understanding the relationship between science and society, but because of the controversial nature of the topics covered in bioethics courses, different groups of students may experience identity conflicts or discomfort when learning about them. However, no previous studies have investigated the impact of undergraduate bioethics students’ experiences in bioethics courses on their opinions and comfort. To fill this gap in knowledge, we investigated undergraduate bioethics students’ attitudes about and comfort when learning abortion, gene editing, and physician assisted suicide, as well as how their gender, religious, and political identity influence their attitudes and changes in their attitudes after instruction. We found that religious students were less supportive of gene editing, abortion, and physician assisted suicide than nonreligious students, non-liberal students were less supportive of abortion and physician assisted suicide than liberal students, and women were less supportive of abortion than men. Additionally, we found that religious students were less comfortable than nonreligious students when learning about gene editing, abortion, and physician assisted suicide, and non-liberal students were less comfortable than liberal students when learning about abortion. When asked how their comfort could have been improved, those who felt that their peers or instructors could have done something to increase their comfort most commonly cited that including additional unbiased materials or incorporating materials and discussions that cover both sides of every controversial issue would have helped them to feel more comfortable when learning about gene editing, abortion, and physician assisted suicide. Finally, we found that students who were less comfortable learning about abortion and physician assisted suicide were less likely to participate in discussions regarding those topics. Our findings show that students in different groups not only tend to have different support for controversial topics like gene editing, abortion, and physician assisted suicide, but they also feel differentially comfortable when learning about them, which in turn impacts their participation. We hope that this work helps instructors to recognize the importance of their students’ comfort to their learning in bioethics courses, and from this study, they can take away the knowledge that students feel their comfort could be most improved by the incorporation of additional inclusive materials and course discussions regarding the controversial topics covered in the course.

In this paper we study the four-point correlation function of the energy–momentum supermultiplet in theories with N = 4 superconformal symmetry in four dimensions. We present a compact form of all component correlators as an invariant of a particular abelian subalgebra of the N = 4 superconformal algebra. This invariant is unique up to a single function of the conformal cross-ratios which is fixed by comparison with the correlation function of the lowest half-BPS scalar operators. Our analysis is independent of the dynamics of a specific theory, in particular it is valid in N = 4 super Yang–Mills theory for any value of the coupling constant. We discuss in great detail a subclass of component correlators, which is a crucial ingredient for the recent study of charge-flow correlations in conformal field theories. We compute the latter explicitly and elucidate the origin of the interesting relations among different types of flow correlations previously observed in arXiv:1309.1424.

Background: Chemistry and particularly enzymology at surfaces is a topic of rapidly growing interest, both in terms of its role in biological systems and its application in biocatalysis. Existing protein immobilization approaches, including noncovalent or covalent attachments to solid supports, have difficulties in controlling protein orientation, reducing nonspecific absorption and preventing protein denaturation. New strategies for enzyme immobilization are needed that allow the precise control over orientation and position and thereby provide optimized activity.

Methodology/Principal Findings: A method is presented for utilizing peptide ligands to immobilize enzymes on surfaces with improved enzyme activity and stability. The appropriate peptide ligands have been rapidly selected from high-density arrays and when desirable, the peptide sequences were further optimized by single-point variant screening to enhance both the affinity and activity of the bound enzyme. For proof of concept, the peptides that bound to β-galactosidase and optimized its activity were covalently attached to surfaces for the purpose of capturing target enzymes. Compared to conventional methods, enzymes immobilized on peptide-modified surfaces exhibited higher specific activity and stability, as well as controlled protein orientation.

Conclusions/Significance: A simple method for immobilizing enzymes through specific interactions with peptides anchored on surfaces has been developed. This approach will be applicable to the immobilization of a wide variety of enzymes on surfaces with optimized orientation, location and performance, and provides a potential mechanism for the patterned self-assembly of multiple enzymes on surfaces.