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Full-Text Articles in Life Sciences
Blood Coagulation Factor Ix: Purification, Activation, Crystallization, Juliet Mcgill
Blood Coagulation Factor Ix: Purification, Activation, Crystallization, Juliet Mcgill
WWU Honors College Senior Projects
This paper presents readers with an optimized procedure for the purification, activation, and crystallization of selected blood coagulation Factor IX double mutant (FIX_2). Through the completion of this work, we aim to enhance future biochemical and structural studies by providing an easier means for the FIX_2 production, in order to increase understanding of the protein’s function within the blood coagulation cascade. The initiation of the blood coagulation cascade is brought on by activation of inactive Factor VIII (FVIII) protein though contact with tissue factor, the FVIII protein then binds to an activated platelet surface where it must wait for its …
Blood Coagulation Factor Ix: Purification, Isolation, Activation, Alex Macneil
Blood Coagulation Factor Ix: Purification, Isolation, Activation, Alex Macneil
WWU Honors College Senior Projects
This paper attempts to provide an optimized strategy for the purification, activation, and isolation of blood coagulation Factor IX mutants. The goal of this work is to enable future biochemical and structural studies of Factor IX to a gain a better understanding of the structural-functional role this protein plays in the blood coagulation cascade. The orchestration and amplification of the blood coagulation cascade requires the binding of Factor VIII (FVIII) to an activated platelet surface, where it serves as a cofactor to a serine protease, Factor IX (FIX). Factor IX circulates the bloodstream as a catalytically silent multidomain protein1. Like …
Structural Analysis Of Protein-Peptide Interactions, Melody Gao
Structural Analysis Of Protein-Peptide Interactions, Melody Gao
WWU Honors College Senior Projects
Over the last three years in the Amacher lab, I have been fortunate to work on two amazing projects studying protein-peptide interactions: PDZ domains and Class A sortases. Both recognize a certain substrate motif, and we are interested in these proteins' selectivity and promiscuity of their substrate.
Lipid Binding Studies Of Blood Coagulation Factor Viii C1 And C2 Domains, Rachel L. Blazevic
Lipid Binding Studies Of Blood Coagulation Factor Viii C1 And C2 Domains, Rachel L. Blazevic
WWU Honors College Senior Projects
Blood coagulation factor VIII (fVIII) is an essential cofactor in the mammalian blood-clotting cascade. fVIII must bind the phospholipid membrane of activated platelets to function as a cofactor for fIXa. The blood coagulation cascade culminates in the formation of a stable blood clot. In humans, the C1 and C2 domains are implicated in binding phospholipid membranes, however the relative contribution of different residues in the lipid-binding mechanism is unclear. Using site-directed mutagenesis, expression of the isolated C1 and C2 domains in Escherichia coli cells, protein purification with metal affinity chromatography, electrospray ionization mass spectrometry, enzyme-linked immunosorbent assays, liposome sedimentation assays, …
Smart Stimulation: Zoo Conservation For 21st Century Zoos, Lauren Retallack
Smart Stimulation: Zoo Conservation For 21st Century Zoos, Lauren Retallack
WWU Honors College Senior Projects
According to a 1992 survey, "an estimated 102 million people, more than attend professional football, baseball, and basketball games combined, visit 162 accredited North American zoos and aquariums each year" (2). People frequent zoos for a variety of reasons, from entertaining children for a few hours, to learning about the wildlife which inhabits their region and foreign places. Regardless of intent, once at the zoo, visitors are presented with a unique opportunity to learn about conservation and the plights of endangered species. It is the job of zoo directors, keepers, staff, and volunteers to get people thinking about conservation while …