A Tablet-Based Application to Enhance Social Connectedness for Individuals With a Cognitive Impairment: Results From the PRISM-CI Pilot Study.

Social engagement is fundamental to successful aging and linked to better emotional, physical, and cognitive health. Maintaining social engagement is challenging for many older adults but especially for those with a cognitive impairment (CI). Information and communication technologies (ICT) can provide enhanced opportunities for social and cognitive engagement for older adults with a CI via increased information, education, and social connectivity access.

Combining an Elastic Network With a Coarse-Grained Molecular Force Field: Structure, Dynamics, and Intermolecular Recognition.

Structure-based and physics-based coarse-grained molecular force fields have become attractive approaches to gain mechanistic insight into the function of large biomolecular assemblies. Here, we study how both approaches can be combined into a single representation, that we term ELNEDIN. In this representation an elastic network is used as a structural scaffold to describe and maintain the overall shape of a protein and a physics-based coarse-grained model (MARTINI-2.

Expression and biophysical analysis of two double-transmembrane domain-containing fragments from a yeast G protein-coupled receptor.

Fragments of G protein-coupled receptors (GPCRs) are widely used as models to investigate these polytopic integral-membrane, signal-transducing molecules, but have proven difficult to prepare in quantities necessary for NMR analyses. We report on the biosynthesis of two double transmembrane (TM) containing fragments of Ste2p, the alpha-factor GPCR from the yeast Saccharomyces cerevisiae. Ste2p(G31-T110) [TM1-TM2] and Ste2p(R231-S339) [TM6-TM7-CT40] were expressed as TrpDeltaLE fusion proteins in Escherichia coli and released by CNBr cleavage.

Thermodynamic basis for promiscuity and selectivity in protein-protein interactions: PDZ domains, a case study.

Like other protein-protein interaction domains, PDZ domains are involved in many key cellular processes. These processes often require that specific multiprotein complexes be assembled, a task that PDZ domains accomplish by binding to specific peptide motifs in target proteins. However, a growing number of experimental studies show that PDZ domains (like other protein-protein interaction domains) can engage in a variety of interactions and bind distinct peptide motifs.