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Published on: 16/09/2019
Biomolecules
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1.
What is a co-enzyme?
2.
Define protein.
3.
Name some secondary metabolites which are useful for human.
4.
Write name of some common protein found in human food.
5.
Define amino acids.
6.
Can you describe what happens when milk is converted into curd or yoghurt, from your understanding of proteins?
7.
What is meant by tertiary structure of proteins?
8.
How are prosthetic groups different from cofactors?
9.
Nucleotides are phosphorylated nucleosides. Justify.
10.
Identify the lipid molecule that is crystallisable in nature. Also, give the name of the disorder produced by it in the human body.
11.
What is trihydroxy propane commonly called? Write its structural formula.
12.
Name of the product formed by esterification of glycerol with a fatty acid. Also draw its structure.
13.
Glycine and alanine are different with respect to one substituent on the \(\alpha -\) carbon. What are the other common substituent groups?
14.
Arrange the following carbohydrates in the order of increasing complexity of chemical structures - fructose, starch, oligosaccharide, maltose, triose.
15.
Proteins have been called 'biological polymers' Explain.
1.
Co-enzymes are organic compounds and their association with the apoenzyme is only transient, usually occurring during the course of catalysis.
2.
Proteins are linear chains of amino acids linked by peptide bonds.
3.
Rubber, Spices, Drugs, Pigments, etc.
4.
Casein. Found in milk
Albumin. Found in eggs.
5.
Amino acids are organic compounds containing an amino group and an acidic group as substituents on the same carbon i.e., the ex-carbon. Hence, they are called ex-amino acids.
6.
Casein is the predominant phosphoprotein, that accounts for nearly 80% of proteins in cow milk and cheese. Milk-clotting proteases act on the soluble portion of the caseins, K-Casein, thus originating an unstable micellar state that results in clot formation. When coagulated with chymosin, casein is sometimes called paracasein. Casein is not coagulated by heat. It is precipitated by acids and by rennet enzymes, a proteolytic enzyme typically obtained from the stomachs of calves.
7.
Tertiary structure:
The overall shape of a single protein molecule; the spatial relationship of the secondary structures to one another. Tertiary structure is generally stabilized by nonlocal interactions, most commonly the formation of a hydrophobic core, but also through salt bridges, hydrogen bonds, disulfide bonds, and even post-translational modifications. The term "Tertiary structure" is often used as synonymous with the term fold. The tertiary structure is what controls the basic function of the protein.
8.
Differences between prosthetic groups cofactors are
| prosthetic group | cofactors |
| It is the non-protien part or the group which gets permanently attached to the enzyme |
It is the non-protein substance or group which gets attached to the enzyme,temporarily or permanently |
| prosthetic groups are organic factors,but some are metallic also like iron,prophyrin of the cytochromes | These can be organic,inorganic or metallic factors |
9.
A nucleoside consists of a nitrogen base and a pentose sugar, but when a phosphate is added to the nucleoside, it is called nucleotide, hence, a nucleotide is a phosphorylated nucleoside.
10.
Cholesterol is a crystallisable lipid of high molecular weight which possesses 17 carbon nucleus of four fused hydrocarbon rings (cyclopentane perhydrophenanthrene) and a long side chain. Cholesterol is insoluble in water and therefore, when cholesterol level rises in blood, it tends to get deposited in the wall of arteries. This causes arteriosclerosis.
11.
Trihydroxy propane is commonly known as glycerol. Its general formula is
\({ CH }_{ 2 }OH-CH(OH)-{ CH }_{ 2 }OH\)
12.
On esterification, triglyceride is produced.
Fatty acids can be metabolised for energy by tissues or stored as energy in the form of triglycerides. The stored triglycerides are digested in response to energy demands, and the unsaturated fatty acids are released into the circulatory system and delivered to the tissues.

13.
There are four substituent groups occupying the four valency positions in an amino acid. These are hydrogen, carboxyl group, amino group and a variable group designated a R group. The R group in amino acid glycine is a hydrogen and a methyl group in case of amino acid alanine, etc.
14.
Triose, fructose, maltose, oligosaccharide and starch.
15.
All the cells are basically made up of proteins. Enzymes which carry out biological reaction are also proteinaceous in nature. Antibodies, haemoglobin and proteinaceous receptors are all proteins. Therefore, they are called as biological polymers.
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