Research has shown that international students experience acculturation stress while adjusting to life in the U.S., resolving over time. However, acculturation stress can be exacerbated by several factors, leading to a negative impact on academic performance and general wellness. Asian international students traditionally underutilize counseling services on campuses. This article reviews the literature of the experiences of Asian international students studying in the U.S. The author offers Confucianism as a cultural consideration to explain cross-cultural challenges experienced by Asian international students and their campus community. Suggestions to support Asian international students are made based on findings of the literature review.

No abstract

Thermostable proteins are advantageous in industrial applications, as pharmaceuticals or biosensors, and as templates for directed evolution. As protein-design methodologies improve, bioengineers are able to design proteins to perform a desired function. Although many rationally designed proteins end up being thermostable, how to intentionally design de novo, thermostable proteins is less clear. UVF is a de novo-designed protein based on the backbone structure of the Engrailed homeodomain (EnHD) and is highly thermostable (T m > 99°C vs. 52°C for EnHD). Although most proteins generally have polar amino acids on their surfaces and hydrophobic amino acids buried in their cores, protein engineers followed this rule exactly when designing UVF. To investigate the contributions of the fully hydrophobic core versus the fully polar surface to UVF’s thermostability, we built two hybrid, chimeric proteins combining the sets of buried and surface residues from UVF and EnHD. Here, we determined a structural, dynamic, and thermodynamic explanation for UVF’s thermostability by performing 4 μ s of all-atom, explicit-solvent molecular dynamics simulations at 25 and 100°C, Tanford-Kirkwood solvent accessibility Monte Carlo electrostatic calculations, and a thermodynamic analysis of 40 temperature runs by the weighted-histogram analysis method of heavy-atom, structure-based models of UVF, EnHD, and both chimeric proteins. Our models showed that UVF was highly dynamic because of its fully hydrophobic core, leading to a smaller loss of entropy upon folding. The charged residues on its surface made favorable electrostatic interactions that contributed enthalpically to its thermostability. In the chimeric proteins, both the hydrophobic core and charged surface independently imparted thermostability.

Study abroad is one aspect of global movement that connects individuals of diverse backgrounds. Individuals studying abroad are proffered to negotiate self-identity when they confront novelty and new contexts. This study chose to use the qualitative method of phenomenological interviews to examine how individuals experience themselves and others when abroad. Specifically, the study focused on modifications of self-identity via self-images. The results presented emotions, cognitions, and behaviors experienced by individuals during global encounters. The study indicates that individuals negotiate identity while studying abroad and modify self-images associated with personal identity (unique character traits) rather than social identity (shared traits with ingroup). The authors propose that identity among global citizens is an ongoing process that is context dependent and less stable than previously regarded.

residues important for peptide specificity and affinity to the PDZ domain. PST's of all eight solved crystal structures of T-cell lymphoma invasion and metastasis 1 (Tiam1) PDZ domains are mapped using knob-socket analyses. The comparison among the PST maps of all Tiam1 PDZ-ligand structures reveal determinants of peptide affinity and specificity. The PST maps of PDZ complexes allow categorization of the important interactions between ligand and the PDZ domain binding pockets. Interestingly, all the ligands bind as a 6 th sheet to the PDZ's 5-strand b-sheet. The extension of the b-sheet provides additional knobs and sockets to pack with PDZ's second a-helix H2. In agreement with previous experimental analyses, the peptide P 0 and P -2 positions directly interact with the PDZ domain, but the binding is more complex. Comparison between different PDZ domains and their respective peptides show that the P 0 position packs primarily against the first coil, and the P -2 position packs into H2. Therefore, the peptide interaction with a PDZ domain can be separated into 3 distinct interactions: 1) extend the b-sheet, 2) interactions of this extended b-sheet with the ahelix H2 (specifically P -2 ), and 3) P 0 packing into the first coil. This set of rules provides a simple yet discrete guide to designing better binding peptides to a PDZ domain. Moreover, this result demonstrates the utility of the Knob-Socket construct in the analysis and design of peptide ligand binding with a protein domain.