amount of activated protein C in the body (Tazbir, 2004). Protein C is a soluble and vitamin K dependent (Toussaint and Gerlach, 2009) molecule that are produced in our body which aids in the prevention of blood clotting. These proteins are initially in an inactive form, and are being activated when thrombin binds to thrombomodulin (Tazbir, 2004). Protein C are able to act as an anticoagulant which inhibit clotting factors Va and VIIIa when it work together with its cofactor protein S (Yamakawa et al
Pathophysiology Intaventricular hemorrhage (IVH) is bleeding in the fragile capillaries that develop in the early months of prenatal development and grow stronger the last ten months of a pregnancy. There are four different degrees based on the bleeding and the areas that are damaged. Preterm infants are at a greater risk for bleeding during events that may cause fluctuations in cerebral blood flow because their blood vessels are not yet fully developed. When IVH occurs, the blood may rupture
No matter the job, stress will always play a role in an individual’s life. Regardless of whether one is a waitress, a teacher, a corrections officer, or a doctor, avoiding stress in the workplace is nearly impossible, perhaps even impossible. And the effects of stress in the workplace are numerous. Stress can have both psychological and physical effects on the members of the workforce. And while the specific effect may differ from one individual to the next, and in particular the effect on physical
The Nature of Proteins Proteins consist of carbon, hydrogen, oxygen and also nitrogen. Proteins are macromolecules. They are constructed from one or more unbranched chains of amino acids; that is, they are polymers ( Compound whose molecule consists of many repeated units linked together). A typical protein contains 200-300 amino acids but some are much smaller (the smallest are often called peptides) and some much larger. Amino Acids Amino acids are the building blocks (monomers)
proximal hairpin loop requires the recruitment of proteins such at TAT and P-TEFb. Currently supporting, but oversimplified, models tell us that Tat bind to the hairpin loop created by the Tar sequence of the HIV LTR, which then recruits P-TEFb. Through the use of CDK9, p-TEFb then phosphorylates Ser2 of the CTD, and allow for elongation. Nevertheless, it has been found that another protein called TCERG1 is involved in Ser 2 phosphorylation. This protein, originally called CA150 (2), has been characterized
sure it stays on its correct course, even assisting in apoptosis. The TP53 gene sends signals to make a protein called tumor protein p53 (or p53). This protein is the tumor suppressor itself, it regulates cell division by keeping cells from proliferating too fast or uncontrollably. The p53 protein is located at the nucleus of all cells in the body, and it binds directly with DNA. Human protein p53 is a phosphoprotein; it has a very specific structure closely related to its function. The
Potential application in food industry There is a great promise of application of ice structuring proteins in food that are frozen. Ice structuring proteins can inhibit re-crystallization during freezing storage, transport and thawing, thus preserving food texture by retarding cellular damage and minimal loss of nutrients (for fruit and vegetables like strawberries, raspberries, tomatoes) by reducing drip (Griffith and Ewart, 1995, Feeney and Yeh, 1998, Breton et al., 2000, Wang, 2000). Re-crystallization
Life Science ORT Papain Enzyme Mitchell Fieldgate Introduction: Enzymes in general are very interesting to learn from and are fundamental in carrying out processes in various organisms. Enzymes are proteins that control the speed of reactions, they help quicken the rate of the reaction and also help cells to communicate with each other. There are 3 main groups of enzymes, first are the metabolic enzymes that control breathing, thinking, talking, moving, and immunity. Next are the digestive enzymes
CONCENTRATION GRADIENT Thickness of gas exchange surface Protein Structure Proteins are made up of amino acids • Primary Structure • Secondary Structure • Tertiary Structure • Quaternary Structure Primary Structure – Chain of Amino Acids COOH – Carboxylic acid group NH2 – Amine Group Condensation – Loss of H20 (joining of acids) Hydrolysis – Gain of H20 (splitting of acid chain) Peptide bond formed in condensation reaction (p for protein) Each time an Amino Acid joins the chain there is
cause an increased uptake of cations and water, which would cause the cell to lyse. The unique composition and structure of the red blood cell membrane allows the cell to selectively pass nutrients and ions into and out of the cell. The lipids and proteins located on opposite sides of the membrane are different, an arrangement that is termed asymmetric, and allows for the selective passage of molecules into and out of the cell ... ... middle of paper ... ...ts duty of delivering oxygen to the tissues
explanation is that PrP(c), the normal isoform of the prion protein, is forced to fold into PrPSc, the other pathological isoform, causing the misfolded PrP(c) to acquire protease-resistance. As to a physical presentation, a clumped protein consisting primarily of alpha-helices (spirals) is converted into one consisting primarily of beta-sheets (sets of pleated hairpins). In an essence, alpha-helical content decreases while beta-sheet content increases. The newly converted protein then possesses the same
as, UBQLN2, VCP/CDC48 in the UPS and SQSTM1/p62, VAPB and some of the vesicular traffic proteins in autophagy have been suggesting a fragile capacity of proteostasis in vulnerable neurons (Bedford et al., 2008; Deng et al., 2011; Paine et al., 2013; Johnson et al., 2010). Recent genetic and biochemical study revealed that mutations in a unique PXX repeat region of UBQLN2 which is one of ubiquitin like protein family are causative in ALS. The different mutations of UBQLN2 are present in the typical
Archaea and Eukaryota. The 3D structure of 18 of these enzymes had been determined, and although the extent of sequence varies between 17% and 45%, all the enzymes have a common (β/α)8-barrel motif, and two catalytic glutamate residues located at the C-terminal end of β-strands 4 and 7, which may give a clue about the mechanism of these enzymes. The Human Cytosolic β-glucosidase is a GH1 enzyme and is present in the liver, kidney, intestine and spleen. It have the same (β/α)8-barrel fold characteristic
1.a. The organelles labelled Y are called Ribosomes, They are attached to the endoplasmic reticulum. The ribosomes make proteins for use in the cell and hold together all components of protein synthesis. The endoplasmic Reticulum spreads all through the cytoplasm and has a large surface area for the attachment of many ribosomes. Also newly synthesised proteins are stored and packaged into vesicles. 1.b. Structure X is called a nuclear pore (A sophisticated entry and exit control system that allows
albicans morphogenesis, and host-fungal interactions. I discovered that upon being phagocytized by macrophages, C. albicans pierce the phagolysosome by inducing hyphae by up-regulating cAMP/PKA pathway. But, before dying, macrophages induce the expression of IL-6, IL-1beta, TNF-alpha, and IL-10, which help developing specific Th cells. While in the acidic conditions such as phagolysosome, C. albicans alters the production of quorum sensing molecules to reduce the acidic microenvironment as a survival
on the C-terminal of a gene called BRCA1 (or “Breast Cancer 1, Early Onset Gene”) tumor suppressor. The BRCA1 gene is located on the long (q) arm of chromosome 17 at region 2 band 1, consists of 24 exons and encodes a multidomain protein of 1863 amino acid residues in human2. The BRCA1 proteins produced from BRCA1 gene help preventing cells from growing and dividing too rapidly or in an uncontrolled way3. The family of BRCA1 genes is called RING-type zinc fingers or RNF. The BRCA1 protein is characterized
compartments, allowing only certain molecules to pass. Embedded within this bilayer are proteins which have carry out specific functions. Integral proteins act as pathways for ion and molecules. Peripheral proteins act as cell to cell recognition sites. Transmembrane protein channels and transporters allow nutrients such as sugars and amino acid to enter the cell. Carbohydrates attach to the external surface of integral proteins holds cells together as well as acting as a site where viruses or chemical messengers
Ion channels are macromolecular protein structures which form pores within the membrane of cells to enable the movement of ions into and out of cells, and is the basis of fundamental process such as establishing a resting potential, generation of action potentials etc. In order for the channel to be involved in these cell functions it must possess certain features such as ionic specificity, gating mechanism (i.e. voltage or ligand binding), for these reasons, channels have been the subject of much
complementation system introduces both temporal and special control of site specific recombination using Cre recombinase enzyme. This system solved many drawbacks have emerged during the extensive use of Cre recombinase in molecular biology. The complemented protein is almost as efficient as the Full CRE in the recombination activity (~95%). Moreover, each fragment lacks the recombinase activity. This system allows precise genetic manipulation. It has a special importance in neuroscience lacking selective promoter
diagnosed with progeria. The patient’s average life expectancy is 13 years of age. However, some that are fortunate surpass this expectancy (Rathore). Progeria is in a group of rare genetic disorders, called laminopothies, which affects genes that encode proteins. Some diseases associated within this group are muscular dystrophy, lipodystrophy, leukodystrophy, diabetes and others. Malfunctioning of the arteries, or arteriosclerosis, is the leading cause of death in progeria. There are plenty of symptoms identified