BIOLOGY PROJECT PDF FILE

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For example, the human body turns over its own weight in ATP each day. Thermodynamics The energies of the stages of a chemical reaction. Substrates need a lot of energy to reach a transition state, which then decays into products.

The enzyme stabilizes the transition state, reducing the energy needed to form products. As all catalysts, enzymes do not alter the position of the chemical equilibrium of the reaction. Usually, in the presence of an enzyme, the reaction runs in the same direction as it would without the enzyme, just more quickly.

Furthermore, enzymes can couple two or more reactions, so that a thermodynamically favorable reaction can be used to "drive" a thermodynamically unfavorable one. For example, the hydrolysis of ATP is often used to drive other chemical reactions. Enzymes catalyze the forward and backward reactions equally. They do not alter the equilibrium itself, but only the speed at which it is reached. For example, carbonic anhydrase catalyzes its reaction in either direction depending on the concentration of its reactants.

Under these conditions the enzyme will, in fact, only catalyze the reaction in the thermodynamically allowed direction. Kinetics Mechanism for a single substrate enzyme catalyzed reaction. The enzyme E binds a substrate S and produces a product P. Enzyme kinetics is the investigation of how enzymes bind substrates and turn them into products. The rate data used in kinetic analyses are obtained from enzyme assays. In Victor Henri proposed a quantitative theory of enzyme kinetics, but his experimental data were not useful because the significance of the hydrogen ion concentration was not yet appreciated.

Their work was further developed by G. Briggs and J. Haldane, who derived kinetic equations that are still widely used today. The major contribution of Henri was to think of enzyme reactions in two stages. In the first, the substrate binds reversibly to the enzyme, forming the enzyme-substrate complex.

The enzyme then catalyzes the chemical step in the reaction and releases the product. Saturation curve for an enzyme reaction showing the relation between the substrate concentration S and rate v. Enzymes can catalyze up to several million reactions per second. For example, the uncatalyzed decarboxylation of orotidine 5'monophosphate has a half life of 78 million years. However, when the enzyme orotidine 5'phosphate decarboxylase is added, the same process takes just 25 milliseconds.

Enzyme rates depend on solution conditions and substrate concentration. Conditions that denature the protein abolish enzyme activity, such as high temperatures, extremes of pH or high salt concentrations, while raising substrate concentration tends to increase activity.

To find the maximum speed of an enzymatic reaction, the substrate concentration is increased until a constant rate of product formation is seen.

Saturation happens because, as substrate concentration increases, more and more of the free enzyme is converted into the substratebound ES form. At the maximum velocity Vmax of the enzyme, all the enzyme active sites are bound to substrate, and the amount of ES complex is the same as the total amount of enzyme.

However, Vmax is only one kinetic constant of enzymes. The amount of substrate needed to achieve a given rate of reaction is also important. This is given by the Michaelis-Menten constant Km , which is the substrate concentration required for an enzyme to reach one-half its maximum velocity.

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Each enzyme has a characteristic Kmfor a given substrate, and this can show how tight the binding of the substrate is to the enzyme. Another useful constant is kcat, which is the number of substrate molecules handled by one active site per second. This is also called the specificity constant and incorporates the rate constants for all steps in the reaction. Because the specificity constant reflects both affinity and catalytic ability, it is useful for comparing different enzymes against each other, or the same enzyme with different substrates.

At this point every collision of the enzyme with its substrate will result in catalysis, and the rate of product formation is not limited by the reaction rate but by the diffusion rate.

Enzymes with this property are called catalytically perfect or kinetically perfect. Inhibition Competitive inhibitors bind reversibly to the enzyme, preventing the binding of substrate. On the other hand, binding of substrate prevents binding of the inhibitor. Substrate and inhibitor compete for the enzyme. The coenzyme folic acid left and the anti-cancer drug methotrexate right are very similar in structure. As a result, methotrexate is a competitive inhibitor of many enzymes that use folates.

Competitive inhibition In competitive inhibition, the inhibitor and substrate compete for the enzyme i.

Often competitive inhibitors strongly resemble the real substrate of the enzyme. For example, methotrexate is a competitive inhibitor of the enzyme dihydrofolate reductase, which catalyzes the reduction of dihydrofolate to tetrahydrofolate. The similarity between the structures of folic acid and this drug are shown in the figure. Uncompetitive inhibition In uncompetitive inhibition the inhibitor can not bind to the free enzyme, but only to the EScomplex.

The EIS-complex thus formed is enzymatically inactive. This type of inhibition is rare, but may occur in multimeric enzymes. Non-competitive inhibition Non-competitive inhibitors can bind to the enzyme at the binding site at the same time as the substrate,but not to the active site.

Because the inhibitor can not be driven from the enzyme by higher substrate concentration in contrast to competitive inhibition , the apparent Vmax changes. But because the substrate can still bind to the enzyme, the Km stays the same.

Mixed inhibition This type of inhibition resembles the noncompetitive, except that the EIS-complex has residual enzymatic activity. This type of inhibitor does not follow Michaelis-Menten equation. In many organisms inhibitors may act as part of a feedback mechanism. If an enzyme produces too much of one substance in the organism, that substance may act as an inhibitor for the enzyme at the beginning of the pathway that produces it, causing production of the substance to slow down or stop when there is sufficient amount.

This is a form of negative feedback. Enzymes which are subject to this form of regulation are often multimeric and have allosteric binding sites for regulatory substances.

Irreversible inhibitors react with the enzyme and form a covalent adduct with the protein. The inactivation is irreversible.

These compounds include eflornithine a drug used to treat the parasitic disease sleeping sickness.

Penicillin and Aspirin also act in this manner. With these drugs, the compound is bound in the active site and the enzyme then converts the inhibitor into an activated form that reacts irreversibly with one or more amino acid residues.

Uses of inhibitors Since inhibitors modulate the function of enzymes they are often used as drugs. An common example of an inhibitor that is used as a drug is aspirin, which inhibits the COX1 and COX-2 enzymes that produce the inflammation messenger prostaglandin, thus suppressing pain and inflammation.

However, other enzyme inhibitors are poisons. For example, the poison cyanide is an irreversible enzyme inhibitor that combines with the copper and iron in the active site of the enzymecytochrome c oxidase and blocks cellular respiration. Biological function Enzymes serve a wide variety of functions inside living organisms. They are indispensable for signal transduction and cell regulation, often via kinases and phosphatases.

They also generate movement, with myosin hydrolysing ATP to generate muscle contraction and also moving cargo around the cell as part of the cytoskeleton. Other ATPases in the cell membrane are ion pumps involved in active transport. Enzymes are also involved in more exotic functions, such as luciferase generating light in fireflies.

Viruses can also contain enzymes for infecting cells, such as the HIV integrase and reverse transcriptase, or for viral release from cells, like the influenza virus neuraminidase.

An important function of enzymes is in the digestive systems of animals. Enzymes such as amylases and proteases break down large molecules starch or proteins, respectively into smaller ones, so they can be absorbed by the intestines. Starch molecules, for example, are too large to be absorbed from the intestine, but enzymes hydrolyse the starch chains into smaller molecules such as maltose and eventually glucose, which can then be absorbed. Different enzymes digest different food substances.

In ruminants which have herbivorous diets, microorganisms in the gut produce another enzyme, cellulase to break down the cellulose cell walls of plant fiber. Several enzymes can work together in a specific order, creating metabolic pathways. In a metabolic pathway, one enzyme takes the product of another enzyme as a substrate. After the catalytic reaction, the product is then passed on to another enzyme. Sometimes more than one enzyme can catalyze the same reaction in parallel, this can allow more complex regulation: with for example a low constant activity being provided by one enzyme but an inducible high activity from a second enzyme.

Gl functions in ycolytic enzymes and their the metabolic pathway of glycolysis Enzymes determine what steps occur in these pathways. Without enzymes, metabolism would neither progress through the same steps, nor be fast enough to serve the needs of the cell. Indeed, a metabolic pathway such as glycolysis could not exist independently of enzymes.

Glucose, for example, can react directly with ATP to become phosphorylated at one or more of its carbons. In the absence of enzymes, this occurs so slowly as to be insignificant.

However, if hexokinase is added, these slow reactions continue to take place except that phosphorylation at carbon 6 occurs so rapidly that if the mixture is tested a short time later, glucosephosphate is found to be the only significant product. Consequently, the network of metabolic pathways within each cell depends on the set of functional enzymes that are present. Control of activity There are five main ways that enzyme activity is controlled in the cell.

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Enzyme production transcription and translation of enzyme genes can be enhanced or diminished by a cell in response to changes in the cell's environment. For example, bacteria may become resistant to antibiotics such as penicillin because enzymes called betalactamases are induced that hydrolyse the crucial beta-lactam ring within the penicillin molecule.

Enzymes can be compartmentalized, with different metabolic pathways occurring in different cellular compartments. Enzymes can be regulated by inhibitors and activators. For example, the end product s of a metabolic pathway are often inhibitors for one of the first enzymes of the pathway usually the 3. Biology project. Upcoming SlideShare. Like this document? Why not share!

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I certify that this project is up to my expectations and as per the guidelines issued by C. Aim of the project: Symptoms of high blood sugar include frequent urination, increased thirst, and increased hunger.

If left untreated, diabetes can cause many complications. Acute complications can include diabetic ketoacidosis , hyperosmolar hyperglycemic state, or death.

Serious long-term complications include cardiovascular disease, stroke, chronic kidney disease, foot ulcers, and damage to the eyes. Specialty Endocrinology Symptoms Frequent urination, increased thirst, increased hunger Complications Diabetic ketoacidosis , nonketotic hyperosmolar coma, heart disease, stroke, chronic kidney failure, foot ulcers Diagnostic method High blood sugar Treatment Healthy diet, physical exercise Medication Insulin, metformin Frequency million 8.

There are three main types of diabetes mellitus: This form was previously referred to as "insulin-dependent diabetes mellitus" IDDM or "juvenile diabetes". The cause is unknown. As the disease progresses alack of insulin may also develop. This form was previously referred to as "non insulin-dependent diabetes mellitus" NIDDM or "adult-onset diabetes". The most commoncause is excessive bodyweight and not enough exercise.

Symptoms may develop rapidly weeks or months in type 1 DM, while they usually develop much more slowly and may be subtle or absent in type 2 DM. Several other signs and symptoms can mark the onset of diabetes although they are not specific to the disease.

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In addition to the known ones above, they include blurry vision, headache, fatigue, slow healing of cuts, and itchy skin. Prolonged high blood glucose can cause glucose absorption in the lens of the eye, which leads to changes in its shape, resulting in vision changes.

A number of skin rashes that can occur in diabetes are collectively known as diabetic dermadromes. This type can be further classified as immune-mediated or idiopathic.

The majority of type 1 diabetes is of the immune-mediated nature, in which a T cell- mediated autoimmune attack leads to the loss of beta cells and thus insulin.

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Most affected people are otherwisehealthy and of a healthy weight when onset occurs. Sensitivity and responsiveness to insulin are usually normal, especially in the early stages.

Type 1 diabetes can affect children or adults, but was traditionally termed "juvenilediabetes" becausea majority of these diabetes cases were in children. A number of lifestyle factors are known to be important to the development of type 2 DM, including obesity defined by a body mass index of greater than 30 , lack of physicalactivity, poor diet, stress, and urbanization.

Even thosewho are not obese often have a high waist—hip ratio. A positive result, in the absence of unequivocal high blood sugar, should be confirmed by a repeat of any of the abovemethods on a different day.

Itis preferable to measurea fasting glucoselevel because of the ease of measurement and the considerabletime commitment of formalglucose tolerance testing, which takes two hours to complete and offers no prognostic advantageover the fasting test.

Dietary changes known to be effective in helpingto prevent diabetes includemaintaininga diet rich in whole grains and fiber, and choosing good fats, such as the polyunsaturatedfats found in nuts, vegetable oils, and fish. Limiting sugary beverages and eating less red meat and other sources of saturated fat can also help prevent diabetes.No two people have exactly the same DNA sequence except for identical twins.

Third, whenever possible, create each output file using a temporary name, and then rename the file after it is complete.

There were two types of conducting systems in the earliest plants systems that have become characteristic of vascular plants as a group. In this way, the population of meristem cells is continually renewed. This is known as the "hierarchical shotgun" approach.

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