3 research outputs found
Identifying Sleep Disorders and Proper Sleep Hygiene in School-Aged Children
Sleep is a daily struggle for many people. Children in particular often suffer from sleep restriction and poor sleep hygiene. Poor sleep can have a negative impact on their physical, social and emotional health. Children in our community are rarely educated about sleep disorders or sleep hygiene. The goal of this project was to create a learning tool to help facilitate sleep education in children.https://scholarworks.uvm.edu/fmclerk/1124/thumbnail.jp
The Charitable Habits of Blood Donors
Introduction: There is a need for a constant supply of blood and blood products (e.g. plasma and platelets) in the American health care system. Common recipients of blood include: patients at risk for major hemorrhage, patients with sickle cell anemia, patients undergoing surgery, and thrombocytopenia in neonatal patients. This demand is met through nationwide blood banks, such as the American Red Cross, and their blood donation programs. The American Red Cross relies solely on volunteer donors; thus, one of the most pressing issues facing this institution is getting donors in the door. Through our survey questions we hope to uncover more factors that guide individuals in their philanthropic ways. The overall goal of this research is focused on unveiling new information that will supply the American Red Cross with valuable insight into their donor population and possible opportunities for joint publicity. We investigated the similarities and difference between how and why individuals undertake certain charitable activities.https://scholarworks.uvm.edu/comphp_gallery/1206/thumbnail.jp
Intein-Promoted Cyclization of Aspartic Acid Flanking the Intein Leads to Atypical N‑Terminal Cleavage
Protein splicing
is a post-translational reaction facilitated by an intein, or intervening
protein, which involves the removal of the intein and the ligation
of the flanking polypeptides, or exteins. A DNA polymerase II intein
from <i>Pyrococcus abyssi</i> (<i>Pab</i> PolII
intein) can promote protein splicing <i>in vitro</i> on
incubation at high temperature. Mutation of active site residues Cys1,
Gln185, and Cys+1 to Ala results in an inactive intein precursor,
which cannot promote the steps of splicing, including cleavage of
the peptide bond linking the N-extein and intein (N-terminal cleavage).
Surprisingly, coupling the inactivating mutations to a change of the
residue at the C-terminus of the N-extein (N-1 residue) from the native
Asn to Asp reactivates N-terminal cleavage at pH 5. Similar “aspartic
acid effects” have been observed in other proteins and peptides
but usually only occur at lower pH values. In this case, however,
the unusual N-terminal cleavage is abolished by mutations to catalytic
active site residues and unfolding of the intein, indicating that
this cleavage effect is mediated by the intein active site and the
intein fold. We show via mass spectrometry that the reaction proceeds
through cyclization of Asp resulting in anhydride formation coupled
to peptide bond cleavage. Our results add to the richness of the understanding
of the mechanism of protein splicing and provide insight into the
stability of proteins at moderately low pH. The results also explain,
and may help practitioners avoid, a side reaction that may complicate
intein applications in biotechnology