Postintensive Care Syndrome: Feasibly Bridging Care at a Tertiary Trauma Center.

Background: Advancements in critical care management have improved mortality rates of trauma patients; however, research has identified physical and psychological impairments that remain with patients for an extended time. Cognitive impairments, anxiety, stress, depression, and weakness in the postintensive care phase are an impetus for trauma centers to examine their ability to improve patient outcomes.

Objective: This article describes one center's efforts to intervene to address postintensive care syndrome in trauma patients.

Adult golf cart injuries: A rising hazard off the course.

Objective: Golf carts are increasingly being used as a means of transportation for travel in neighborhoods, city areas, and unpaved surfaces. The catchment area of our regional trauma center has seen an increase in golf cart use for transportation. In fact, Georgia has recently changed legislation to support the growing need for more defined laws around golf cart use.

Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p.

Yeast Hho1p contains two domains, GI and GII, that are homologous to the single globular domain of the linker histone H1 (GH1). We showed previously that the isolated GI and GII domains have different structural stabilities and functional properties. GI, like GH1 and the related GH5, is stably folded at low ionic strength (10 mM sodium phosphate) and gives strong protection of chromatosome-length DNA ( approximately 166 bp) during micrococcal nuclease digestion of chromatin.

Distinct protein interfaces in transmembrane domains suggest an in vivo folding model.

Given the known high-resolution structures of alpha-helical transmembrane domains, we show that there are statistically distinct classes of transmembrane interfaces which relate to the folding and oligomerization of transmembrane domains. Distinct types of interfaces have been categorized and refer to those between: the same polypeptide chain, different polypeptide chains, helices that are sequential neighbors, and those that are nonsequential. These different interfaces may reflect different phases in the mechanism of transmembrane domain folding and are consistent with the current experimental evidence pertaining to the folding and oligomerization of transmembrane domains.

Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p.

The Saccharomyces cerevisiae homologue of the linker histone H1, Hho1p, has two domains that are similar in sequence to the globular domain of H1 (and variants such as H5). It is an open question whether both domains are functional and whether they play similar structural roles. Preliminary structural studies showed that the two isolated domains, GI and GII, differ significantly in stability.

Identification of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A proteomic and genomic analysis.

In a recent bioinformatic analysis, we predicted the presence of multiple families of cell surface glycosylphosphatidylinositol (GPI)-anchored proteins (GAPs) in Arabidopsis (G.H.H.

Prediction of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A genomic analysis.

Glycosylphosphatidylinositol (GPI) anchoring of proteins provides a potential mechanism for targeting to the plant plasma membrane and cell wall. However, relatively few such proteins have been identified. Here, we develop a procedure for database analysis to identify GPI-anchored proteins (GAP) based on their possession of common features.