biomoleculesWHERE cd.courseId=2 AND cd.subId=7 AND chapterSlug='biomolecules' and status=1SELECT ex_no,page_number,question,question_no,id,chapter,solution FROM question_mgmt as q WHERE courseId='2' AND subId='7' AND chapterId='12' AND ex_no!=0 AND status=1 ORDER BY ex_no,CAST(question_no AS UNSIGNED)

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Chapter 9 : Biomolecules


As discussed above the organism is made of cells. They perform vital function. The cells are made of organic macromolecule through these number of metabolic activities that occur and lead the building block of our body. These biomolecules are carbohydrate, protein, lipids, vitamins, nucleic acid etc. In this chapter we will get information regarding the linkage of carbohydrate i.e. glycosidic bond , protein linkage ie. peptide bond and more. Only 20 amino acids are yet known as the combination as these 20 amino acids make millions of proteins, protein are the building block unit of the cell. Emphasis on nucleic acid on how these formed their structure and functions.

Exercise 1
Q:
A:

Macromolecules are large complex molecules present in colloidal state in intercellular fluid. They are formed by the condensation of low molecular weight micromolecules and hence are polymeric in nature.

Polysaccharides, proteins, and nucleic acids are common examples of macromolecules.


Exercise 1
Q:
A:

(a) Glycosidic bond is formed normally between C-1 and C-4, of adjacent monosaccharide units.

Glycosidic bond

(b) Peptide bond is a covalent bond that is formed between two adjacent amino acids by condensation of NH2 gp of ane amino acid and cp oh gp of other amino acid and hence it can be depicted as

P

II - OH

C

Peptide bond

(c) Phosphodiester bond is a strong covalent bond formed between phosphate and two adjacent sugar groups. Such bonds form the sugar phosphate backbone of nucleic acids.

Phosphodiester bond


Exercise 1
Q:
A:

The helical polypeptide chain undergoes coiling and folding to form a complex three-dimensional shape referred to as tertiary structure of proteins. These coiling and folding hide the non-polar amino acid chains in the interior of molecule and expose the polar side chains to the exterior. The tertiary structure is held together by the weak non-covalent interacting formed between various parts of the polypeptide chain.


Exercise 1
Q:
A:

 (a)

 

Molecule

Structure

1.

Adenosine

Adenosine

2.

Thymidine

Thymidine

3.

Sucrose

Sucrose

           Glucose                             Fructose

4.

Maltose

Maltose

5.

Lactose

Lactose

           Galactose                                                      Glucose                    

6.

Ribose

Ribose

7.

DNA

DNA

8.

RNA

RNA

9.

Glycerol

Glycerol

10.

Insulin

Insulin

(b)

 

Compound

Manufacturer

Buyer

1.

Starch products

Kosha Impex (P) Ltd.

Research laboratories, educational institutes, and other industries, which use biomolecules as a precursor for making other products.

2.

Liquid glucose

Marudhar apparels

 

3.

Various enzymes such as amylase, protease, cellulase

Map (India) Ltd

 


Exercise 1
Q:
A:

Yes, if we are given a method to know the sequence of proteins, we can use this information to determine purity of a protein. It is known that an accurate sequence of a certain amino acid is very important for the functioning of a protein. If there is any change in the sequence, it would alter its structure, thereby altering the function. So by knowing sequence of a given protien, we can determine its structure and compare it with any of the known correct protein sequence. Any change in the sequence can be linked to the purity or homogeneity of a protein.

For example, a single change in the sequence of haemoglobin in P chain at 6th position can alter the normal haemoglobin structure to an abnormal structure that can cause sickle cell anaemia.


Exercise 1
Q:
A:

Proteins used as therapeutic agents are as follows:

1. Thrombin and fibrinogen – They help in blood clotting.

2. Antigen (antibody) – It helps in blood transfusion.

3. Insulin – It helps in maintaining blood glucose level in the body.

4. Renin – It helps in osmoregulation.

Proteins are also commonly used in the manufacture of cosmetics, toxins, and as biological buffers.


Exercise 1
Q:
A:

Triglyceride which is formed by esprification of a single molecule of glycerol, with three molecules of fatty acids. It is mainly present in vegetable oils and animal fat.

Structure of triglyceride

               Structure of triglyceride

These three fatty acids can be same or different.


Exercise 1
Q:
A:

Like lactobacillus. These bacteria secrete lactic acid which changes the Ph of milk and proteins are very sensitive to change in Ph. So this changed Ph to destruction of secondary and tertiary structures of protein (called denaturation). Which leads to precipitation of milk proteins and lead to curd formation.

Milk has many globular proteins. Milk is converted into curd or yoghurt by action of bacteria.


Exercise 1
Q:
A:

Ball and stick models are 3-D molecular models that can be used to describe the structure of biomolecules.

In ball and stick model, the atoms are represented as balls whereas the bonds that hold the atoms are represented by the sticks. Double and triple bonds are represented by springs that form curved connections between the balls. The size and colour of various atoms are different and are depicted by the relative size of the balls. It is the most fundamental and common model of representing biomolecular structures.

biomolecular structures

In the above ball and stick model of D-glucose, the oxygen atoms are represented by red balls, hydrogen atoms by blue balls, while carbon atoms are represented by grey balls.


Exercise 1
Q:
A:

Titrating a neutral or basic amino acid against a weak base will dissociate only one functional group, whereas titration between acidic amino acid and a weak base will dissociate two or more functional groups.


Exercise 1
Q:
A:

Structure of alanine

Structure of alanine


Exercise 1
Q:
A:

Gums are hetero-polysaccharides. They are made from two or more different types of derived monosaccharides. On the other hand, fevicol is polyvinyl alcohol (PVA) glue. It is not a polysaccharide.


Exercise 1
Q:
A:

(a) Test for protein

Biuret’s test – If Biuret’s reagent is added to protein, then the colour of the reagent changes from light blue to purple.

(b) Test for fats and oils

Grease or solubility test

(c) Test for amino acid

Ninhydrin test – If Ninhydrin reagent is added to the solution, then the colourless solution changes to pink, blue, or purple, depending on the amino acid.

Item

Name of the test

Procedure

Result

Inference

1.

Fruit juice

Biuret’s test

Fruit juice + Biuret’s reagent

Colour changes from light blue to purple

Protein is present.

 

 

Grease test

To a brown paper, add a few drops of fruit juice.

No translucent spot

Fats and oils are absent or are in negligible amounts.

 

 

Ninhydrin test

Fruit juice + Ninhydrin reagent + boil for 5 minutes

Colourless solution changes to pink, blue, or purple colour

Amino acids are present.

2.

Saliva

Biuret’s test

Saliva + Biuret’s reagent

Colour changes from light blue to purple

Proteins are present.

 

 

Grease test

On a brown paper, add a drop of saliva.

No translucent spot

Fats/oils are absent.

 

 

Ninhydrin test

Saliva + Ninhydrin reagent + boil for 5 minutes

Colourless solution changes to pink, blue, or purple colour

Amino acids are present.

3.

Sweat

Biuret’s test

Sweat + Biuret’s reagent

No colour change

Proteins are absent.

 

 

Solubility test

Sweat + Water

Oily appearance

Fats/oil may be present.

 

 

Ninhydrin test

Sweat + Ninhydrin reagent + boil for 5 minutes

No colour change, solution remains colourless

Amino acids are absent.

4.

Urine

Biuret’s test

Few drops of urine + Biuret’s reagent

Colour changes from light blue to purple

Proteins are present.

 

 

Solubility test

Few drops of urine + Water

Little bit of oily appearance

Fats may or may not be present.

 

 

Ninhydrin test

Few drops of urine + Ninhydrin reagent + boil for 5 minutes

Colourless solution changes to pink, blue, or purple colour depending on the type of amino acid

Amino acids are present.

 


Exercise 1
Q:
A:

Approximately, 100 billion tonnes of cellulose are made per year by all the plants in the biosphere and it takes 17 full grown trees to make one ton of paper. Trees are also used to fulfill the other requirements of man such as for timber, food, medicines, etc. Hence, it is difficult to calculate the annual consumption of plant material by man.


Exercise 1
Q:
A:

Properties of enzymes

(1) Enzymes are complex macromolecules with high molecular weight.

(2) They catalyze biochemical reactions in a cell. They help in the breakdown of large molecules into smaller molecules or bring together two smaller molecules to form a larger molecule.

(3) Enzymes do not start a reaction. However, they help in accelerating it.

(4) Enzymes affect the rate of biochemical reaction and not the direction of the reaction.

(5) Most of the enzymes have high turnover number. Turnover number of an enzyme is the number of molecules of a substance that is acted upon by an enzyme per minute under saturated substrate concensation. High turnover number of enzymes increases the efficiency of reaction.

(6) Enzymes are specific in action.

(7) Enzymatic activity decreases with increase in temperature and all enzymes show maximum activity at an optimum kmp of 30-40 0C.

(8) They show maximum activity at an optimum pH of 6 – 8.

(9) The velocity of enzyme increases with increase in substrate concentration and then, ultimately reaches maximum velocity.


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