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Burgers are probably among the satisfying foods on earth that we celebrate the month of May as the National Burger month. It is enormous how we commemorate an appetizing variation of the meat sandwich that the world loves so much. You can also take this occasion to indulge in more burgers than you normally would.
Some burgers are cooked rare while others go well-done. There are burgers piled high with crisp toppings and served on warm buns, and there are also those made for plain sandwich filling. In addition to the classic ground beef burgers, there are other meats used to form patties appropriate for grilling.
Of all the meat used, buffalo burgers preserve the likable meaty flavor of ground beef, but are more expensive than their beef counterparts. However, Buffalo meat is measured the healthier meat in general because of the more natural farming methods, compared to the more commercial ground beef.
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Corey and Audrina enjoyed a cheery picnic together this week — confirming quite a change of heart for the BMX rider who had some hostile, fighting words for Audrina when they split in March. “A girl that’s told yes by everyone surrounding them grows up to be a heartless closed off insecure individual. Some woman will always be empty & rotten from the inside out. U cant love a heartless woman,” he tweeted about her at the time.
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To maximize your intake of health-enhancing nutrients like vitamin C to grow taller, carotenoids (beta-carotene, lycopene, lutein, zeaxanthin), folate, potassium, fibre, and antioxidant-rich plant compounds like flavonoids, you need to reach for at least seven, ideally closer to 10, servings of fruits and vegetables each day. One serving consists of:
• 1 medium-size fruit or vegetable (an apple, orange, carrot or pear)
• 1/2 cup (125 mL) raw, cooked or frozen fruit or vegetable (a scoop of cooked peas or a small bowl of sliced peaches)
• 1/2 cup (125 mL) juice (a small glass of orange or tomato juice)
• 1 cup (250 mL) salad (a small side salad)
• 1/4 cup (60 mL) dried fruit (a medium-size handful of raisins)
For those of you who think this sounds like a truckload of fruits and vegetables, let me assure you it’s only a wheelbarrow full (just kidding!). It’s easier than you think:
1. Never miss a meal. Include at least one to two servings of fruits or veggies at every meal and at snack times. This is so important! Most people simply can’t meet their daily quota any other way to grow taller.
Looking for a brighter future to grow taller? Try eating a diet rich in colorful fruits and vegetables. The potential benefits associated with eating more fruits and vegetables stack up quickly: Reducing your risk of certain chronic diseases is only the beginning.
Whether fresh, frozen, canned, dried or 100% juice, these 200+ taste sensations are quick, delicious and convenient, and will keep you healthy all year round to grow taller.
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This March, forget about UCLA taking on Duke in the NCAA finals. There’s an even more important battle going on right here–between big-name contenders from broccoli to turnips. The goal: to determine which vegetable is No. 1 in nutrition, and which should take first place when you’re eating your food. Of course, all veggies are winners when it comes to warding off excess weight and preventing disease; but with all the peeling and chopping you have to do to get them to the table, they’re not the easiest foods around (no wonder most women fail to score five servings a day) to grow taller.
A natural relaxant, helps alleviate insomnia by inducing normal sleep; reduces anxiety and depression and stabilizes mood; helps in the treatment of migraine headaches helps the immune system function properly; aids in weight control by reducing appetite; enhances the release of growth hormones; helps control hyperactivity in children.
A powerful anti-oxidant and a good source of sulfur, which prevents disorders of the hair, skin, and nails; assists the breakdown of fats, thus helping to prevent a buildup of fat in the liver and arteries, that might obstruct blood flow to the brain, heart, and kidneys; helps to detoxify harmful agents such as lead and other heavy metals; helps diminish muscle weakness; prevents brittle hair; protects against the affects of radiation; beneficial for women who take oral contraceptives because it promotes the excretion of estrogen; reduces the level of histamine in the body which can cause the brain to relay wrong messages; helpful to individuals suffering from schizophrenia.
Amino Acids are the chemical units or “building blocks” of the body that make up proteins. Protein substances make up the muscles, tendons, organs, glands, nails, and hair. Growth, repair and maintenance of all cells are dependent upon them. Next to water, protein makes up the greatest portion of our body weight. Amino Acids that must be obtained from the diet are called “Essential Amino Acids” other Amino Acids that the body can manufacture from other sources are called “NonEssential Amino Acids.”
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Humans can produce 10 of the 20 amino acids. The others must be supplied in the food. Failure to obtain enough of even 1 of the 10 essential amino acids, those that we cannot make, results in degradation of the body’s proteins—muscle and so forth—to obtain the one amino acid that is needed. Unlike fat and starch, the human body does not store excess amino acids for later use—the amino acids must be in the food every day.
The 10 amino acids that we can produce are alanine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline, serine and tyrosine. Tyrosine is produced from phenylalanine, so if the diet is deficient in phenylalanine, tyrosine will be required as well. The essential amino acids are arginine (required for the young, but not for adults), histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. These amino acids are required in the diet. Plants, of course, must be able to make all the amino acids. Humans, on the other hand, do not have all the the enzymes required for the biosynthesis of all of the amino acids.
A member of a group of organic polymers containing chains of amino acids linked together by peptide bonds. Proteins play a vital part in the structure and function of all cells, comprising 10-30% of cell mass. Structurally, they are divided into two main groups: fibrous proteins and globular proteins. Functionally, they have many varied roles, acting as enzymes, hormones, respiratory pigments, and antibodies. Excess protein cannot be stored in the body and is excreted, mainly as urea in the urine. Each gram of protein contains about 4 kcal of energy. Protein can supply up to 10% of the energy needed to sustain an endurance activity. A diet containing 30-15% of calories from protein should be adequate for most athletes. The World Health Organization recommend a daily protein intake of l g kg body weight−1: studies by sports nutritionists indicate that athletes involved in prolonged heavy training require more protein, about 1.2-1.7 g kg body weight−1. There is little scientific evidence to support the use of very high-protein diets by athletes. On the contrary, these diets could damage the kidneys, and can cause dehydration and constipation. Protein-rich foods include meat, grains, and legumes.
The unloading of oxygen is also facilitated by cooperativity, such that after one oxygen molecule is released, the other three soon follow. This assures that the tissues will receive maximum oxygen once it is delivered. Alpha-hemoglobin by itself, or tetramers of all beta subunits, also bind oxygen, but not with the same cooperativity. Such evidence indicates that there is some form of molecular interaction between the subunits of the tetramer of adult hemoglobin.
Protein consumed in foods is digested in the stomach and small intestine into amino acids which are absorbed into the bloodstream and taken to the liver for initial processing. Some amino acids are transported to muscles and tissues where they are rebuilt into protein. According to the UK Dietary Reference Values, the amount of protein sufficient for most individuals aged 19 or over is 0.75 g per kg per day (about 45 g for the average female and 55.5 g for the average male). Those who are very active, suffering from severe illness, or recovering from surgery need more protein. For example, in a report of an international conference on Foods, Nutrition and Soccer Performance held in Zurich in 1994, sports nutritionists stated that soccer players require between 1.4 to 1.7 grams of protein per kilogram body weight. Protein requirements are also relatively high in children, pregnant women, and nursing mothers. Very active people can meet the body’s demands for extra protein by having a well-balanced diet adjusted to their higher energy requirements. Attempts to increase muscle size artificially by consuming excessively high protein diets are thought by most dietitians to be useless. As protein in the diet increases, proportionately less is absorbed from the intestine. Amino acids not needed for growth or repair of body tissues are broken down and excreted as urea, or converted into either glucose (to be used as an energy source) or body fat. One gram of protein yields about 4 Calories. Protein can supply up to 10 per cent of the energy needed to sustain prolonged exercise.
Consumption of excess protein may cause dehydration and constipation, and can lead to obesity. It may also cause deficiencies in vitamin B6, and a loss of calcium with an increased risk of osteoporosis, but these effects are not fully established. Protein deficiency causes profound weight loss, mental and physical retardation in children, oedema, and anaemia.
Many subtle variations in a particular protein can be generated by making amino acid replacements at specific positions in the polypeptide sequence. For example, at any specific position an amino acid can be replaced by another to generate a mutant protein that may have different characteristics by virtue of the single replaced amino acid. Amino acids can also be deleted from a protein sequence, either individually or in groups. These proteins are referred to as deletion mutants. Deletion mutants may or may not be missing one or more functions or properties of the full, naturally occurring protein. Moreover, part or all of a protein sequence can be joined or fused to that of another protein. The resulting protein is called a hybrid or fusion protein, which generally has characteristics that combine those of each of the joined partners.
Many such designs involve making small changes in already existing proteins: for example, by changing three amino acids in an enzyme often used to improve detergents’ cleaning power, commercial biochemists have doubled the enzyme’s stability in wash water. Medical applications of designer proteins seem especially promising. For instance, we might one day cure cancer by combining portions of one protein that recognizes cancer with part of another protein that attacks it. One of the challenges facing such a development, however, is the problem of designing a protein that attacks only cancer cells and not healthy ones.
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These are just a very few of the many applications of proteins, including a very familiar one, discussed in more depth at the conclusion of this essay: nutrition. Given the importance and complexity of proteins, it might be hard to imagine that they can be produced artificially, but, in fact, such production is taking place at the cutting edge of biochemistry today, in the field of “designer proteins.”
The four blood types (A, B, AB, and O) are differentiated on the basis of the proteins present in each. This is only one of many key roles that proteins play where blood is concerned. If certain proteins are missing, or if the wrong proteins are present, blood will fail to clot properly, and cuts will refuse to heal.
One particularly important type of protein is an enzyme, discussed in the essay on that topic. Enzymes make possible a host of bodily processes, in part by serving as catalysts, or substances that speed up a chemical reaction without actually participating in, or being consumed by, that reaction. Enzymes enable complex, life-sustaining reactions in the human body—reactions that would be too slow at ordinary body temperatures—and they manage to do so without forcing the body to undergo harmful increases in temperature.
The steps involved in folding and the shape that finally results are determined by such chemical properties as hydrogen bonds, electrical attraction between positively and negatively charged side chains, and the interaction between polar and nonpolar molecules. Non Polar molecules are called hydrophobic, or “water-fearing,” because they do not mix with water but instead mix with oils and other substances in which the electric charges are more or less evenly distributed on the molecule. Polar molecules, on the other hand, are termed hydrophilic, or “water-loving,” and mix with water and water-based substances in which the opposing electric charges occupy separate sides, or ends, of the molecule.
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The distinction between the two is partly historical: secondary structures are those that were first discerned by scientists of the 1950s, using the techniques and knowledge available then, whereas an awareness of tertiary structure emerged only later. Finally, quaternary structure indicates the way in which many protein chains associate with one another. For example, hemoglobin consists of four protein chains (spirals, actually) of two slightly different types, all attached to an iron atom.
The specific properties of each kind of protein are largely dependent on the kind and sequence of the amino acids in it, yet many proteins include components other than amino acids. For example, some may have sugar molecules (sugars are discussed in the essay on Carbohydrates) chemically attached. Exactly which types of sugars are attached and where on the protein chain attachment occurs vary with the specific protein.
Most of us recognize the term protein in a nutritional context as referring to a class of foods that includes meats, dairy products, eggs, and other items. Certainly, proteins are an important part of nutrition, and obtaining complete proteins in one’s diet is essential to the proper functioning of the body. But the significance of proteins extends far beyond the dining table. Vast molecules built from enormous chains of amino acids, proteins are essential building blocks for living systems—hence their name, drawn from the Greek proteios, or “holding first place.
Any of a group of complex organic macromolecules that contain carbon, hydrogen, oxygen, nitrogen, and usually sulfur and are composed of one or more chains of amino acids. Proteins are fundamental components of all living cells and include many substances, such as enzymes, hormones, and antibodies, that are necessary for the proper functioning of an organism. They are essential in the diet of animals for the growth and repair of tissue and can be obtained from foods such as meat, fish, eggs, milk, and legumes.
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Balance carbs and protein. Cutting back on highly processed carbohydrates and increasing protein improves levels of blood triglycerides and HDL, and so may reduce your chances of having a heart attack, stroke, or other form of cardiovascular disease. It may also make you feel full longer, and stave off hunger pangs.
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