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Chapter 3 biology protein structure
Structure of protein essay
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Recommended: Chapter 3 biology protein structure
With development of technology, scientist found that protein is an important composition of human body cells and tissues. In other words, Protein is the main part and participate in almost every process in intracellular organisms. The Protein is the most abundant biological macromolecule, which is the material basis of life, to be more precisely, is the essential organic building blocks of cells of living organisms and it provides the main bearer of life activities from bacteria to human beings. The protein is a substance that making by coiling and folding one or more certain spatial structure of polypeptide chains which are amino acids joined together by peptide bond that through the " dehydration condensation " approach to composition formed …show more content…
Protein’s structure contain primary, that is amino acid sequence forming a polypeptide chains; secondary, that is the folding of a polypeptide chain, resulting in an alpha helix, beta-pleated sheet or a random coil structure; tertiary, that is completely folding of the sheets and helices of a secondary structure held in position by hydrophobic and hydrophilic interactions; quaternary, that is the assembly of multiple folded protein molecules in a multi-subunitcomplex. The protein folding is a physical process to form a functional three-dimensional structure. However, protein is usually random coil into specific functional structure, it is possible that misfolding happen and it will cause inactive protein that means not only loss its biological function but also give a toxic function(Fabrizio et al,2006). These essay will discuss the role of protein failure to fold and clump together that cause several neurodegenerative diseases, including CJD, Parkinson’s and Alzheimer’s …show more content…
Yet diverse diseases affected in distinct regions of the brain, which result in divergent clinical manifestations. Neuronal loss is progressed cell death or apoptosis, there are at least three hypotheses to explain this phenomenon. The widely accepted hypothesis is the gain-of-toxic-activity that the protein misfolding and aggregation result in neurotoxicity. The direct evidence is misfolded proteins aggregation in vitro can cause neuronal apoptosis( Claudio, 2003). This theory of the amyloid beta-protein neurotoxicity have four kinds of interpretation. The first one, it is possible that extracellular aggregated protein may interact with specific receptors, which activation of a signaling pathway that can lead to apoptosis. The second one is intracellular aggregated protein cause recruitment of cellular factors and then damage the cells. The third one is the amyloid beta-protein and prion protein to form neurotoxicity due to formation of ion channels cause the membrane rupture and depolarization that result in changing the ionic homeostasis and the regulation of cell signaling, leading to cell death. The fourth one is the aggregation of the protein caused by oxidative stress, through the generating of free radicals, causing protein, lipid oxidation and increasing the intracellular calcium ion concentration and then the
Abstract: Bovine spongiform encephalopathy is caused by a prion, which is an infectious agent comprised solely of protein. The prion is a degenerate form of a normal cellular protein found in the brain and in nervous tissue. It targets the normal protein and causes the normal protein to change its shape. When enough of the prion is produced, the cell dies and symptoms of the disease are expressed.
In the subsequent essay I will discuss and explain the relative function of the Prion protein. The Prion protein, also known as PrPC, ‘’is a membrane-anchored protein with two N-glycosylation sites and, although it is highly expressed in the nervous tissues, its physiological functions have yet to be well established’’ (Coordination Chemistry Reviews). PrPC/PrP is found in healthy brains in this form, and consists of 250 Amino Acids, yet after a simple misfolding in the secondary structure; this can alienate the PrP and forms PrPsc, which is the abnormal form of the Prion protein. The infectious agent PrPsc causes neuropathological changes in the brain, and instantly places the individual under the category of someone with the prion disease. PrPsc forms insoluble fibres and thus cannot be studied well using Nuclear Mass Resonance (NMR), and it is also more resistant to protease digestion. Furthermore, ‘’ The transmissible spongiform encephalopathies (TSEs) arise from conversion of the membrane-bound prion protein from PrPC to PrPSc, the latter being the scrapie form. Examples of the TSEs include mad cow disease, chronic wasting disease in deer and elk, scrapie in goats and sheep, and kuru and Creutzfeldt-Jakob disease in humans’’ (http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2904554/. 2014). The following diagram shows the conversion from PrPc to PrPsc:
Proteins are one of the main building blocks of the body. They are required for the structure, function, and regulation of the body’s tissues and organs. Even smaller units create proteins; these are called amino acids. There are twenty different types of amino acids, and all twenty are configured in many different chains and sequences, producing differing protein structures and functions. An enzyme is a specialized protein that participates in chemical reactions where they serve as catalysts to speed up said reactions, or reduce the energy of activation, noted as Ea (Mader & Windelspecht).
Neurodegeneration is used mainly for diseases that are characterised by progressive loss of structure and function of neurons. There are many neurodegenerative diseases including amyotrophic lateral sclerosis that...
Prions are the causative agents of a few rapidly progressive neurodegenerative diseases known as transmissible spongiform encephalopathies, or prion diseases. These are infectious isoforms of a host-encoded cellular protein known as the prion protein. Prion diseases affect humans and animals and are uniformly fatal in nature. [1]
clumps of abnormal proteins insides the brain cells. These proteins are called the Tau proteins they take a form of picks bodies. This slowly leads to frontotemporal dementia.
Protein have connection with amino acid to help in functions of: skin, muscle, hair and bones
Scientists know that Alzheimer disease is characterized by a gradual spread of sticky plaques and clumps of tangled fibers that disrupt the organization of nerve cells in the brain. However , a definite cause, prevention, or cause has not been found.
Thesis/Preview Statement – Alzheimer’s disease (AD) causes a decline in brain function, it destroys healthy nerve cells. Today, we have discussed Causes, Symptoms, and Diagnosis of AD.
Alzheimer’s disease or AD is an incurable disorder of the brain that results in loss of normal brain structure and function. In an AD brain, normal brain tissue is slowly replaced by structures called plaques and neurofibrillary tangles. The plaques represent a naturally occurring sticky protein called beta amyloid and in an Alzheimer’s brain, sufferer’s tend to accumulate too much of this protein. Neurofibrillary tangles represent collapsed tau proteins which, in a normal brain along with microtubules, form a skeleton that maintains the shape of the nerve cells. In Alzheimer’s disease, the tau proteins break loose from their normal location and form tangles. Without the support of these molecules, nerve cells collapse and die. As normal brain structure is lost with progression of the disease, brain function also degenerates. Patients afflicted with Alzheimer’s disease display a gradual mental decline. Initially, and most apparently, there is a loss of short-term memory. Eventually, as a patient progresses to later stages of the disease, the brain becomes so damaged that patients can no longer communicate or recognize immediate family or even themselves. They have difficulty walking and standing and frequently fall. In the final stages, they lose bladder and bowel control and have difficulty with swallowing, frequently leaving them malnourished and dehydrated. Eventually, they are forced to remain bedridden and, without the help of life-prolonging measures provided in a hospital, die. However, this level of deterioration is severe and may take as long as twenty years. Because of the disease’s slow progress and its usual later start in a person’s life, a victim of AD will usually die first of natural causes. Under the objectives ...
Alzheimer’s disease comes from the last name of a neuro-psychiatrist from Germany, Alois Alzheimer. The disease was first diagnosed when a woman in her early fifties began experience memory problems. “Alzheimer recounted the now famous case of ‘Auguste D.’ a 51-year-old housewife who had been failing mentally for several years. As a result she had been admitted to his care in the Asylum for the Insane and Epileptic…” (Maurer and Maurer 1). After her death, he continued to examine her brain to find causes and explanations for her behavior. He discovered “…classic neuro-pathological signs of plaques and tangles” (Maurer and Maurer 1). “Plaques are chains of amino acids that are pieces of the amyloid precursor protein…tangles are aggregates of the protein tau” (Secko 1). As plaques develop they produce tangles and “these two abnormalities ultimately lead to loss of cognitive function” (Secko 1) Alois Alzheimer’s research has allowed many specialist to conclude that the apolipoproetein E gene may contribute to the disease.
When eaten, protein is broken down into amino acids. Proteins and amino acids are used for almost every metabolic process in the body, and are the building blocks for every tissue in your body.
Scientists, coaches, and athletes have recognized that periodized strength training promotes increase in skeletal muscle size, increase in force, and increase of the regenerating capacity of the muscle cells.
Alzheimer’s Disease is named after a German doctor, who specializes in the brain and nervous system, named Alois Alzheimer. This Disease forms in the brain. Alzheimer’s is the most common form of Dementia, a general term for memory loss and other intellectual abilities serious enough to enter. The Tau protein ensures the tubes in your brain stay straight allowing molecules to pass through freely. In Alzheimer’s Disease the protein collapses into strands or tangles, making the tubes disintegrate. There is visible differences of brain tissue in the from misfolded proteins called plaques and tangles. Beta-Amyloid clumps block signals and communication between cells in the brain. Researchers agree that Alzheimer’s Disease is m...
As they always say HEALTH IS WEALTH! Your food selection today, makes you enjoy for the moment and affects your health tomorrow and in the future!