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NAME: Amelia Singh (812000718)

Dietary supplements

Omega 3 – Fish Oil

What is Fish Oil?

Fish oil can be obtained from eating fish or by taking supplements. The fish used as sources do not actually produce omega-3 fatty acids, but instead accumulate them by consuming either microalgae or prey fish that have accumulated omega-3 fatty acids, together with a high quantity of antioxidants such as iodide and selenium, from microalgae, where these antioxidants are able to protect the fragile polyunsaturated lipids from peroxidation. Fish that are especially rich in the beneficial oils known as omega-3 fatty acids include mackerel, tuna, salmon, sturgeon, mullet, bluefish, anchovy, sardines, herring, trout, and menhaden. They provide about 1 gram of omega-3 fatty acids in about 3.5 ounces of fish. They also contain small amounts of vitamin E to prevent spoilage. They might also be combined with calcium, iron, or vitamins A, B1, B2, B3, C, or D. Two of the most important omega-3 fatty acids contained in fish oil are eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA). The American Heart Association (AHA) recommends everyone eat fish (particularly fatty fish) at least twice a week. A safe dose of fish oil that is considered safe is 3 grams daily.

 

What are the claims and benefits of Fish Oil?

  • Preventing heart diseases or strokes
  • Lowers blood pressure or triglyceride levels (fats related to cholesterol)
  • Helps with depression, psychosis, attention deficit-hyperactivity disorder (ADHD), Alzheimer’s disease, and other thinking disorders.
  • Dry eyes, glaucoma, and age-related macular degeneration (AMD), a very common condition in older people that can lead to serious sight problems.
  • Women use it to prevent painful periods; breast pain; and complications associated with pregnancy such as miscarriage, highblood pressure late in pregnancy, and early delivery.
  • Used for diabetes, asthma, developmental coordination disorders, movement disorders, dyslexia, obesity, kidney disease, weak bones (osteoporosis), certain diseases related to pain and swelling such as psoriasis, and preventing weight loss caused by some cancer drugs.
  • used after heart transplant surgery to prevent high blood pressure and kidney damage that can be caused by the surgery itself or by drugs used to reduce the chances that the body will reject the new heart. Fish oil is sometimes used after coronary artery bypass surgery. It seems to help keep the blood vessel that has been rerouted from closing up.

How does it work?

A lot of the benefit of fish oil seems to come from the omega-3 fatty acids that it contains. Interestingly, the body does not produce its own omega-3 fatty acids. Nor can the body make omega-3 fatty acids from omega-6 fatty acids, which are common in the Western diet. A lot of research has been done on EPA and DHA, two types of omega-3 acids that are often included in fish oil supplements.

Omega-3 fatty acids reduce pain and swelling. This may explain why fish oil is likely effective for psoriasis and dry eyes. These fatty acids also prevent the blood from clotting easily. This might make fish oil helpful for some heart conditions.

Why do we need Omega 3 in the Body?

Omega-3 fatty acids (also known as n-3 fatty acids) are polyunsaturated fatty acids that are essential nutrients for health. We need omega-3 fatty acids for numerous normal body functions, such as controlling blood clotting and building cell membranes in the brain, and since our bodies cannot make omega-3 fats, we must get them through food. Omega-3 fatty acids are also associated with many health benefits, including protection against heart disease and possibly stroke. New studies are identifying potential benefits for a wide range of conditions including cancer, inflammatory bowel disease, and other autoimmune diseases such as lupus and rheumatoid arthritis.

References

Metabolomics
First, let’s look at some definitions:
• Metabolites :- these are all the bits and pieces a cell leaves behind; they are known as the intermediates and products of metabolism such as antibiotics, pigments, carbohydrates, fatty acids and amino acids. There are both primary and secondary metabolites
• Metabolome :- These are dynamic set of small-molecule metabolites
• Metabolomics :- In simple terms is basically close examination of a cell and the remnants it leaves behind to make assumptions about its whereabouts. It’s the survey of metabolites in the body, also referred to as a chemical fingerprint.
Metabolomics is a new up and coming field that can assist in early diagnosis, therapy monitoring and fort the understanding the pathogenesis of many diseases. Information rich analytical techniques of NMR (nuclear magnetic resonance) spectroscopy and mass spectrometry (MS)are the most regularly used methods.
Biofilms are any group of microorganisms or bacteria that bind together creating a strong network resisting our arsenal of antibiotics. When these assemble together, no drug can eliminate this biofilm layer which is extremely dangerous if it comes on contact with open wounds which inhibits the ability for the wound to heal; putting the elderly, diabetics and those with compromising weak immune systems at risk which may lead to amputations. When the metabolites are examined by means of detecting chemical signatures via NMR and MS, assumptions and conclutions can be made about the state of the cell. Dr. Ammons is currently doing research on getting a better understanding of the lifestyle of biofilms using metabolomics. Knowledge of the energy source of biofilms can be very useful, as this can help in terminating them by cutting off their supply. Or customized macrophages can be designed to digest and destroy them. Novel metabolic mechanisms and therapeutic targets can be uncovered by Dr. Ammons using complex systems biology.
Check out these videos for more info 😀
https://www.youtube.com/watch?v=0DSA_8t4-UA
https://www.youtube.com/watch?v=Lpj5YmscOZE

References
https://biochemistry1362byme.wordpress.com/2014/11/26/metabolomics-studies/
http://www.ncbi.nlm.nih.gov/pubmed/18785810
http://metabolomics.chem.agilent.com/Frontiers/122801-Disease-Research/

There is a specific nutrient called carnitine found in high content in red meat and energy drinks which is being investigated and has experiments being done by Stanley Hazen at the Cleveland Clinic Lerner Research Institute in Ohio and colleagues. The population of gut bugs/bacteria in the body is increased and causes the thickening of the artery walls in a process called atherosclerosis. Atherosclerosis (also known as arteriosclerotic vascular disease or ASVD) is a condition in which an artery wall thickens as a result of the accumulation of fatty materials such as cholesterol and triglyceride. It is a syndrome affecting arteriole blood vessels, a chronic inflammatory response in the walls of arteries, caused largely by the accumulation of macrophage white blood cells and promoted by low density lipoproteins (LDL, plasma proteins that carry cholesterol and triglycerides) without adequate removal of fats and cholesterol from the macrophages by functional high density lipoproteins (HDL). It is commonly referred to as a hardening or furring of the arteries. It is caused by the formation of multiple plaques within the arteries.

Their goal and objective was to prove that the increased intake of red meat and energy drinks containing carnitine increases the risk of heart disease due to increase in gut bacteria population.

Further experiments were then conducted on mice where a diet high in carnitine was fed to let’s say group A of the mice and Group B of the mice were fed the same diet but with suppressed gut flora. Group B, the one fed with less gut flora experienced no atherosclerosis. It was observed that humans with a greater intake of red meat in their diet were at a higher cardiac risk.

Some bacteria in the intestine use this carnitine as their energy source and a waste product called trimethylamine (TMA) is released when breaking it down.  Trimethylamine-N-oxide (TMAO), which is excreted in urine is the substance that the liver then converts it to.

The level of TMAO is increased by the high levels of dietary carnitine, thus TMAO is important as ‘bad’ cholesterol’ are picked up, which are supposed to be destroyed by macrophages (white blood cells) causing the plaque buildup on the walls of the arteries increasing atherosclerosis. Further testing was done comparing the carnitine level found in vegetarians and vegans diet to a diet of a meat-eater suggesting there was more TMA bacteria found in their gut/intestines. “Cut down the frequency and portion sizes.” is what Stanely emphasizes

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IT’S EASY SO……

1) Glycine and proline are the most abundant amino acids in the structure of-

a)Hemoglobin

b) Myoglobin

c) Insulin

d) Collagen

2)Which out of the following amino acids carries a net positive charge at the physiological p H ?

a) Valine

b) Leucine

c) Isoleucine

d) None of the followings.

3) Use the following amino acids to answer the questions below;   ala, asp, arg, val, lys, leu, ser

a.  Which amino acid is most polar?

b.  Which amino acid is most non-polar?

c.  Which amino acid gives an acidic solution?

d.  Which amino acid gives a basic solution?

e.  Which two amino acids form salt bridges between proteins?

f.  Which two amino acids form hydrogen bonds between proteins?

g.  Which two amino acids form hydrophobic interactions in proteins?

4) Which of these things do both plant and animal cells have?

a. Cell wall

b. Chloroplasts

c. Cytoplasm

d. Vacuole

e. Cytoplasm

5) Which of the following correctly matches an organelle with its function?

a. mitochondrion . . . photosynthesis

b. nucleus . . . cellular respiration

c. ribosome . . . manufacture of lipids

d. lysosome . . . movement

e. central vacuole . . . storage

6) Which of the following clues would tell you whether a cell is prokaryotic or eukaryotic?

a. the presence or absence of a rigid cell wall

b. whether or not the cell is partitioned by internal membranes

c. the presence or absence of ribosomes

d. whether or not the cell carries out cellular metabolism

e. whether or not the cell contains DNA

7)Which specialised cell does not have a nucleus?
a. Sperm cell
b. Nerve cell
c. Egg cell
d. Red blood cell
e. White blood cell

8)What is the function of the cell membrane?
a. To control which substances move in and out of the cell
b. To help the cell to keep a firm shape
c. To make food for the cell
d. All of the above
e. To control which substances move in and out of the cell

9)Glucose is a: 

a. Monosaccharide

b. Disaccharide

c. Ploysaccharide

d. Simple sugar

e. Both a monosaccharide and a simple sugar

10) Carbohydrates and fats provide our bodies with energy in the form of calories True/False

11) Which substance allows glucose to be removed from the blood and moved into the cells to be stored as glycogen?

a. Amylase

b. Lipase

c. Insulin

d. Intrinsic factor

12) Muscle glycogen functions to store and export glucose to maintain blood glucose between meals True/False

13) Glucose 6-phosphate dehydrogenase is an NAD+-dependent enzyme True/False 

14) Ribose can not be synthesized in all tissues True/False

15) Which complex carbohydrate is a storage form of energy in plants?

a. cellulose

b. starch

c. glycogen

d. all of the above

😀 ^_^ 🙂

Proteins, from the Greek proteios, meaning first, are a class of organic compounds which are present in and vital to every living cell. In the form of skin, hair, callus, cartilage, muscles, tendons and ligaments, proteins hold together, protect, and provide structure to the body of a multi-celled organism. In the form of enzymes, hormones, antibodies, and globulins, they catalyze, regulate, and protect the body chemistry. In the form of hemoglobin, myoglobin and various lipoproteins, they effect the transport of oxygen and other substances within an organism.
Proteins are generally regarded as beneficial, and are a necessary part of the diet of all animals. Humans can become seriously ill if they do not eat enough suitable protein, the disease kwashiorkor being an extreme form of protein deficiency. Protein based antibiotics and vaccines help to fight disease, and we warm and protect our bodies with clothing and shoes that are often protein in nature (e.g. wool, silk and leather).The deadly properties of protein toxins and venoms is less widely appreciated. Botulinum toxin A, from Clostridium botulinum, is regarded as the most powerful poison known. Based on toxicology studies, a teaspoon of this toxin would be sufficient to kill a fifth of the world’s population. The toxins produced by tetanus and diphtheria microorganisms are nearly as poisonous. A list of highly toxic proteins or peptides would also include the venoms of many snakes, and ricin, the toxic protein found in castor beans.

Protein Structure

PROTEINS are biological polymers composed of amino acids. Amino acids, linked together by peptide bonds, form a polypeptide chain. One or more polypeptide chains twisted into a 3-D shape form a protein. Proteins have complex shapes that include various folds, loops, and curves. Folding in proteins happens spontaneously. Chemical bonding between portions of the polypeptide chain aid in holding the protein together and giving it its shape. There are two general classes of protein molecules: globular proteins and fibrous proteins. Globular proteins are generally compact, soluble, and spherical in shape. Fibrous proteins are typically elongated and insoluble. Globular and fibrous proteins may exhibit one or more of four types of protein structure. These structure types are called primary, secondary, tertiary, and quaternary structure.

Protein Structure Levels

The four levels of protein structure are distinguished from one another by the degree of complexity in the polypeptide chain. A single protein molecule may contain one or more of the protein structure types.

  • Primary Structure – describes the unique order in which amino acids are linked together to form a protein. Proteins are constructed from a set of 20 amino acids. Generally, amino acids have the following structural properties: 
    • A carbon (the alpha carbon) bonded to the four groups below:
    • A hydrogen atom (H)
    • A Carboxyl group (-COOH)
    • An Amino group (-NH2)
    • A “variable” group or “R” group

    All amino acids have the alpha carbon bonded to a hydrogen atom, carboxyl group, and amino group. The “R” group varies among amino acids and determines the differences between these protein monomers. The amino acid sequence of a protein is determined by the information found in the cellular genetic code. The order of amino acids in a polypeptide chain is unique and specific to a particular protein. Altering a single amino acid causes a gene mutation, which most often results in a non-functioning protein.

  • Secondary Structure – refers to the coiling or folding of a polypeptide chain that gives the protein its 3-D shape. There are two types of secondary structures observed in proteins. One type is the alpha (α) helix structure. This structure resembles a coiled spring and is secured by hydrogen bonding in the polypeptide chain. The second type of secondary structure in proteins is the beta (β) pleated sheet. This structure appears to be folded or pleated and is held together by hydrogen bonding between polypeptide units of the folded chain that lie adjacent to one another.
  • Tertiary Structure – refers to the comprehensive 3-D structure of the polypeptide chain of a protein. There are several types of bonds and forces that hold a protein in its tertiary structure. Hydrophobic interactions greatly contribute to the folding and shaping of a protein. The “R” group of the amino acid is either hydrophobic or hydrophilic. The amino acids with hydrophilic “R” groups will seek contact with their aqueous environment, while amino acids with hydrophobic “R” groups will seek to avoid water and position themselves towards the center of the protein. Hydrogen bonding in the polypeptide chain and between amino acid “R” groups helps to stabilize protein structure by holding the protein in the shape established by the hydrophobic interactions. Due to protein folding, ionic bonding can occur between the positively and negatively charged “R” groups that come in close contact with one another. Folding can also result in covalent bonding between the “R” groups of cysteine amino acids. This type of bonding forms what is called a disulfide bridge. Interactions called van der Waals forces also assist in the stabilization of protein structure. These interactions pertain to the attractive and repulsive forces that occur between molecules that become polarized. These forces contribute to the bonding that occurs between molecules.
  • Quaternary Structure – refers to the structure of a protein macromolecule formed by interactions between multiple polypeptide chains. Each polypeptide chain is referred to as a subunit. Proteins with quaternary structure may consist of more than one of the same type of protein subunit. They may also be composed of different subunits. Hemoglobin is an example of a protein with quaternary structure. Hemoglobin, found in the blood, is an iron containing protein that binds oxygen molecules. It contains four subunits: two alpha subunits and two beta subunits.

Protein Structure Determination

The three-dimensional shape of a protein is determined by its primary structure. The order of amino acids establishes a protein’s structure and specific function. The distinct instructions for the order of amino acids are designated by the genes in a cell. When a cell perceives a need for protein synthesis, the DNA unravels and is transcribed into an RNA copy of the genetic code. This process is called DNA transcription. The RNA copy is then translated to produce a protein. The genetic information in the DNA determines the specific sequence of amino acids and the specific protein that is produced. Proteins are examples of one type of biological polymer. Along with proteins, carbohydrates, lipids, and nucleic acids constitute the four major classes of organic compounds in living cells.

 

Also, watch this animation. Although it was not very detailed, you can get a generalized understanding

http://www.wisc-online.com/objects/ViewObject.aspx?ID=ap13304

yes yes…. I know the video is long….. but don’t you just melt when you hear that Indian accent… lol …. I think it is IMPOSSIBLE to fall asleep during one of her lectures …. lol…. XD  But seriously guys… She makes a lot of sense and I understood what she was saying and got additional information as well…. 😀

Amino Acids

An amino acid is an organic molecule that, when linked together with other amino acids, forms a protein. Amino acids are essential to life because the proteins they form are involved in virtually all cell functions. Some proteins function as enzymes, some as antibodies, while others provide structural support. Although there are hundreds of amino acids found in nature, proteins are constructed from a set of 20 amino acids.

Amino Acid Structure

Generally, amino acids have the following structural properties:

  • A carbon (the alpha carbon)
  • A hydrogen atom (H)
  • A Carboxyl group (-COOH)
  • An Amino group (-NH2)
  • A “variable” group or “R” group

Amino Acid Structure

 

All amino acids have the alpha carbon bonded to a hydrogen atom, carboxyl group, and amino group. The “R” group varies among amino acids and determines the differences between these protein monomers. The amino acid sequence of a protein is determined by the information found in the cellular genetic code. The genetic code is the sequence of nucleotide bases in nucleic acid (DNA and RNA) that code for amino acids. These gene codes not only determine the order of amino acids in a protein, but they also determine a protein’s structure and function.

 

 

Amino Acid Groups

Amino acids can be classified into four general groups based on the properties of the “R” group in each amino acid. Amino acids can be polar, nonpolar, positively charged, or negatively charged. Polar amino acids have “R” groups that are hydrophilic, meaning that they seek contact with aqueous solutions. Nonpolar amino acids are the opposite (hydrophobic) in that they avoid contact with liquid. These interactions play a major role in protein folding and give proteins their 3-D structure. Below is a listing of the 20 amino acids grouped by their “R” group properties. The nonpolar amino acids are hydrophobic, while the remaining groups are hydrophilic.Nonpolar Amino Acids

  • Ala: Alanine           Gly: Glycine           Ile: Isoleucine            Leu: Leucine
  • Met: Methionine     Trp: Tryptophan     Phe: Phenylalanine     Pro: Proline
  • Val: Valine

Polar Amino Acids

  • Cys: Cysteine         Ser: Serine            Thr: Threonine
  • Tyr: Tyrosine          Asn: Asparagine     Gln: Glutamine

Polar Basic Amino Acids (Positively Charged)

  • His: Histidine           Lys: Lysine            Arg: Arginine

Polar Acidic Amino Acids (Negatively Charged)

  • Asp: Aspartic acid     Glu: Glutamic acid

While amino acids are necessary for life, not all of them can be produced naturally in the body. Of the 20 amino acids, 10 can be produced naturally. These amino acids are alanine, proline, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, serine, glycine, and tyrosine. The amino acids that can not be produced naturally are called essential amino acids. They are arginine (essential for children), histidine, threonine, isoleucine, methionine, leucine, lysine, phenylalanine, tryptophan, and valine. The essential amino acids must be acquired through diet. Unlike humans, plants are capable of synthesizing all 20 amino acids.

Protein Synthesis

Proteins are produced through the processes of DNA transcription and translation. In protein synthesis, DNA is first copied into RNA. The RNA transcript, messenger RNA (mRNA), is then translated into amino acids. Cell structures called ribosomes along with another RNA molecule called transfer RNA help to translate mRNA into amino acids. Amino acids are joined together through dehydration synthesis, a process in which a peptide bond is formed between the amino acids. A polypeptide chain is formed when a number of amino acids are linked together by peptide bonds. After several modifications, the polypeptide chain becomes a fully functioning protein. One or more polypeptide chains twisted into a 3-D structure form a protein.

Biological Polymers

While amino acids and proteins play an essential role in the survival of living organisms, there are other biological polymers that are also necessary for normal biological functioning. Along with proteins, carbohydrates, lipids, and nucleic acids constitute the four major classes of organic compounds in living cells.

 

HEEYYYY GUUUYYSS!!!!!!! Hope you are not falling asleep on me…. These little guys get to me every time yes….. Hope u liked them as much as i did!!!! and ……..

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