While there is a wide-spread awareness as to why protein is needed for metabolism and health, only a few people realise that continuous and excess consumption of protein can actually harm your body. Before dwelling on why excess protein is harmful, let’s understand what protein is and why you body needs it.
Structurally, protein is a biopolymer. Polymer is any molecule that is made up of individual building blocks that are linked together in repeating units (examples include plastic). Biopolymer is a polymer produced by living organisms (in addition to proteins, examples include DNA). The individual units that form a protein are amino acids. When individual amino acids are linked together, they are called either a polypeptide or a protein. A polypeptide is a chain of three or more amino acids that are linked together. A protein is a polypeptide that has ‘folded’ itself (proteins are among the most complex organic compounds found in nature and ‘protein folding’ is an intricate process; simplistically, when a polypeptide folds, it assumes a three-dimensional shape unlike the polypeptide itself that is two-dimensional). Proteins can be made up of one folded polypeptide or multiple polypeptides. Metaphorically, if a polypeptide is considered a yarn, then protein is a knitted sweater.
Nutritionally, protein is a key macro-nutrient without which there is no life. In fact, amino acids that form proteins are called ‘building blocks of life’ because they are the fundamental structural element of cells in your body. You need protein for growth and maintenance of your body. Apart from water, proteins are the most abundant type of molecules in your body. Protein is the major structural component of your body cells, especially those in the muscles. For example, keratin, a family of fibrous structural proteins, makes up your skin, nails and hair and also gives them their structure. In addition to enhancing growth of your body and its maintenance as well as providing its definite shape, proteins help transport molecules in your body. For example, hemoglobin, the protein that makes up red blood cells in your bloodstream, carries oxygen from your lungs to your body's tissues and returns carbon dioxide from the tissues back to the lungs.
Proteins also facilitate communication between cells that is crucial for maintaining life by carrying a multitude of signals. For example, ‘signal proteins’ such as hormones and neurotransmitters send messages around the body to initiate activities like glucose production and voluntary movements such as walking and lifting things.
In addition, proteins play a key role in body movements, including that of muscles, and molecular transport among cells. For example, while myosin and actin, two motor proteins enable muscle contraction, kinesin, another motor protein, moves chromosomes during cell division.
Besides, proteins help you fight diseases—antibodies that are used by your body’s immune system to fight viruses and bacteria that invade your body are proteins.
Most importantly, proteins work as enzymes to speed up innumerable life-sustaining biochemical reactions in your cells. Some of the biochemical reactions that happen in milliseconds with the help of enzymes would take millions or even billions of years to complete if they are absent. This means without proteins that work as enzymes them essential biological reactions in your body will not happen fast enough for you to stay alive.
Over 500 amino acids have been discovered in nature. However, only 20 serve as constituents of proteins that form tissues in your body. Of these 20, nine are essential amino acids because they cannot be synthesised by your body and must be supplied through your diet. These are phenylalanine, valine, threonine, tryptophan, methionine, leucine, isoleucine, lysine and histidine.
Of the remaining 11 non-essential amino acids (in fact, they are essential for your body but since they are synthesised by your body or derived from essential amino acids, they need not be a part of your diet), six are conditionally essential in your diet—while your body can synthesise these amino acids in normal conditions, it may not be able to produce enough of these to meet your needs when you are sick or your body is under stress. These are arginine, cysteine, glycine, glutamine, proline and tyrosine. The remaining five are dispensable as they can be synthesised by your body. These are alanine, aspartic acid, asparagine, glutamic acid and serine.
Animal sources of protein include meat, fish, eggs and milk as well as milk products such as cheese and yogurt. Staple plant sources of protein include whole grains and cereals such as buckwheat, oats, rye, millet, maize (corn), rice, wheat, bulgar, sorghum, amaranth and quinoa as well as vegetables and leaves, especially legumes, nuts and seeds, beans and peas and fruits. Legumes, some of which are called pulses have higher. Vegetable (or plant) sources of protein with higher concentration of protein include soybeans, lentils, kidney beans, white beans, mung beans, chickpeas, cowpeas, lima beans, pigeon peas, lupines, wing beans, almonds, brazil nuts, cashews, pecans, walnuts, cotton seeds, pumpkin seeds, sesame seeds and sunflower seeds.
Among vegetation food staples toots and tubers such as yams, cassava and sweet potato contain lesser concentration of protein. Fruits, while rich in other essential nutrients, are another poor source of amino acids. Vegetation foods with lesser protein concentration can be complemented with those which are rich in protein to ensure that your meal is balanced. This is especially important for children as protein is essential for enhancing growth.
During digestion, proteins are broken down in the stomach in to amino acids necessary for dietary needs with the help of hydrochloric acid and a group of enzymes called proteases. These amino acids are then absorbed through the intestinal wall (if proteins are not properly broken down before they are absorbed, various health consequences may occur).
Before being absorbed in small intestine, proteins are broken down into single amino acids or peptides of several amino acids in your stomach by hydrochloric acid and pepsin, a digestive enzyme, and in the small intestine by trypsin and chymotrypsin, two other digestive enzymes. Peptides that contain more than four amino acids are not typically absorbed (newborns of mammals have exceptional ability to digest and assimilate protein—they can absorb intact proteins at the small intestine).
The amount of protein required in your diet depends on various factors including your body weight and composition, energy intake, physical activity level and whether you are ill or injured. Physical activity and exertion as well as enhanced muscular mass enhance the need for protein.
While protein is essential for your body, consumption of excess protein can harm your body. If you eat more protein than your body requires, it will simply convert most of those calories to sugar and then fat. Increased blood sugar levels can also feed pathogenic bacteria and yeast, such as Candida albicans (candidiasis), as well as fuel cancer cell growth.
Also, when your protein consumption is excess, your liver removes the amino group from the amino acid and converts it to ammonia which is toxic (the remaining amino acid mostly contains carbon and hydrogen which is used for energy). Ammonia is toxic to the human system, and enzymes convert it to urea or uric acid by addition of carbon dioxide molecules (which is not considered a deamination process) in the urea cycle, which also takes place in the liver. Urea and uric acid can diffuse into the blood and then be excreted in urine.
In a nutshell, consumer of protein beyond a threshold can lead to increased levels of sugar in your body (which can lead to diabetes and a litany of lifestyle diseases) and increased production of ammonia which is toxic and therefore is harmful.
Structurally, protein is a biopolymer. Polymer is any molecule that is made up of individual building blocks that are linked together in repeating units (examples include plastic). Biopolymer is a polymer produced by living organisms (in addition to proteins, examples include DNA). The individual units that form a protein are amino acids. When individual amino acids are linked together, they are called either a polypeptide or a protein. A polypeptide is a chain of three or more amino acids that are linked together. A protein is a polypeptide that has ‘folded’ itself (proteins are among the most complex organic compounds found in nature and ‘protein folding’ is an intricate process; simplistically, when a polypeptide folds, it assumes a three-dimensional shape unlike the polypeptide itself that is two-dimensional). Proteins can be made up of one folded polypeptide or multiple polypeptides. Metaphorically, if a polypeptide is considered a yarn, then protein is a knitted sweater.
Nutritionally, protein is a key macro-nutrient without which there is no life. In fact, amino acids that form proteins are called ‘building blocks of life’ because they are the fundamental structural element of cells in your body. You need protein for growth and maintenance of your body. Apart from water, proteins are the most abundant type of molecules in your body. Protein is the major structural component of your body cells, especially those in the muscles. For example, keratin, a family of fibrous structural proteins, makes up your skin, nails and hair and also gives them their structure. In addition to enhancing growth of your body and its maintenance as well as providing its definite shape, proteins help transport molecules in your body. For example, hemoglobin, the protein that makes up red blood cells in your bloodstream, carries oxygen from your lungs to your body's tissues and returns carbon dioxide from the tissues back to the lungs.
Proteins also facilitate communication between cells that is crucial for maintaining life by carrying a multitude of signals. For example, ‘signal proteins’ such as hormones and neurotransmitters send messages around the body to initiate activities like glucose production and voluntary movements such as walking and lifting things.
In addition, proteins play a key role in body movements, including that of muscles, and molecular transport among cells. For example, while myosin and actin, two motor proteins enable muscle contraction, kinesin, another motor protein, moves chromosomes during cell division.
Besides, proteins help you fight diseases—antibodies that are used by your body’s immune system to fight viruses and bacteria that invade your body are proteins.
Most importantly, proteins work as enzymes to speed up innumerable life-sustaining biochemical reactions in your cells. Some of the biochemical reactions that happen in milliseconds with the help of enzymes would take millions or even billions of years to complete if they are absent. This means without proteins that work as enzymes them essential biological reactions in your body will not happen fast enough for you to stay alive.
Over 500 amino acids have been discovered in nature. However, only 20 serve as constituents of proteins that form tissues in your body. Of these 20, nine are essential amino acids because they cannot be synthesised by your body and must be supplied through your diet. These are phenylalanine, valine, threonine, tryptophan, methionine, leucine, isoleucine, lysine and histidine.
Of the remaining 11 non-essential amino acids (in fact, they are essential for your body but since they are synthesised by your body or derived from essential amino acids, they need not be a part of your diet), six are conditionally essential in your diet—while your body can synthesise these amino acids in normal conditions, it may not be able to produce enough of these to meet your needs when you are sick or your body is under stress. These are arginine, cysteine, glycine, glutamine, proline and tyrosine. The remaining five are dispensable as they can be synthesised by your body. These are alanine, aspartic acid, asparagine, glutamic acid and serine.
Animal sources of protein include meat, fish, eggs and milk as well as milk products such as cheese and yogurt. Staple plant sources of protein include whole grains and cereals such as buckwheat, oats, rye, millet, maize (corn), rice, wheat, bulgar, sorghum, amaranth and quinoa as well as vegetables and leaves, especially legumes, nuts and seeds, beans and peas and fruits. Legumes, some of which are called pulses have higher. Vegetable (or plant) sources of protein with higher concentration of protein include soybeans, lentils, kidney beans, white beans, mung beans, chickpeas, cowpeas, lima beans, pigeon peas, lupines, wing beans, almonds, brazil nuts, cashews, pecans, walnuts, cotton seeds, pumpkin seeds, sesame seeds and sunflower seeds.
Among vegetation food staples toots and tubers such as yams, cassava and sweet potato contain lesser concentration of protein. Fruits, while rich in other essential nutrients, are another poor source of amino acids. Vegetation foods with lesser protein concentration can be complemented with those which are rich in protein to ensure that your meal is balanced. This is especially important for children as protein is essential for enhancing growth.
During digestion, proteins are broken down in the stomach in to amino acids necessary for dietary needs with the help of hydrochloric acid and a group of enzymes called proteases. These amino acids are then absorbed through the intestinal wall (if proteins are not properly broken down before they are absorbed, various health consequences may occur).
Before being absorbed in small intestine, proteins are broken down into single amino acids or peptides of several amino acids in your stomach by hydrochloric acid and pepsin, a digestive enzyme, and in the small intestine by trypsin and chymotrypsin, two other digestive enzymes. Peptides that contain more than four amino acids are not typically absorbed (newborns of mammals have exceptional ability to digest and assimilate protein—they can absorb intact proteins at the small intestine).
The amount of protein required in your diet depends on various factors including your body weight and composition, energy intake, physical activity level and whether you are ill or injured. Physical activity and exertion as well as enhanced muscular mass enhance the need for protein.
While protein is essential for your body, consumption of excess protein can harm your body. If you eat more protein than your body requires, it will simply convert most of those calories to sugar and then fat. Increased blood sugar levels can also feed pathogenic bacteria and yeast, such as Candida albicans (candidiasis), as well as fuel cancer cell growth.
Also, when your protein consumption is excess, your liver removes the amino group from the amino acid and converts it to ammonia which is toxic (the remaining amino acid mostly contains carbon and hydrogen which is used for energy). Ammonia is toxic to the human system, and enzymes convert it to urea or uric acid by addition of carbon dioxide molecules (which is not considered a deamination process) in the urea cycle, which also takes place in the liver. Urea and uric acid can diffuse into the blood and then be excreted in urine.
In a nutshell, consumer of protein beyond a threshold can lead to increased levels of sugar in your body (which can lead to diabetes and a litany of lifestyle diseases) and increased production of ammonia which is toxic and therefore is harmful.
No comments:
Post a Comment