Chemistry

Biomolecules

Question:

Differentiate between globular and fibrous proteins.

Answer:

(i) Fibrous proteins: These proteins consist of linear thread like molecules which tend to lie side by side (parallel) to form fibres. The polypeptide chains in them are held together usually at many points by hydrogen bonds and some disulphide bonds. As a result,intermolecular forces of attraction are very’ strong and hence fibrous proteins are insoluble in water. Further, these proteins are stable to moderate changes in temperature and pH. Fibrous proteins serve as the chief structural material of animal tissues.For example, keratin in skin, hair, nails and wool, collagen in tendons, fibrosis in silk and myosin in muscles.
(ii) Globular proteins: The polypeptide chain in these proteins is folded around itself in such a way so as to give the entire protein molecule an almost spheroidal shape. The folding takes place in such a manner that hydrophobic (non-polar) parts are pushed inwards and hydrophilic (polar) parts are pushed outwards. As a result, water molecules interact strongly with the polar groups and hence globular protein are water soluble. As compared to fibrous proteins, these are very sensitive to small changes of temperature and pH. This class of proteins include all enzymes, many hormones such as insulin from pancreas, thyroglobulin from thyroid gland, etc.

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Biomolecules

Q 1.

The letters ' D ' or ' L' before the name of a stereoisomer of a compound indicate the correlation of configuration of that particular stereoisomer.
ncert-exemplar-problems-class-12-chemistry-biomolecules-21
This refers to their relation with one of the isomers of glyceraldehydes. Predict whether the following compound has ‘D' or ‘L' configuration.

Q 2.

How do enzymes help a substrate to be attacked by the reagent effectively?

Q 3.

Which of the following pairs represents anomers?
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Q 4.

During curdling of milk, what happens to sugar present in it?

Q 5.

Name the linkage connecting monosaccharide units in polysaccharides.

Q 6.

Which monosaccharide units are present in starch, cellulose and glycogen and which linkages link these units?

Q 7.

What are the common types of secondary structure of proteins?

Q 9.

Assertion (A): Vitamin D can be stored in our body.
Reason (R): Vitamin D is fat soluble vitamin.

Q 10.

Which sugar in called invert sugar? Why is it called so?

Q 11.

What is glycogen? How is it different from starch?

Q 12.

What are the hydrolysis products of (i) sucrose, and (ii) lactose?

Q 13.

Why does compound (A) given below not form an oxime?
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Q 14.

What are essential and non-essential amino acids? Give two examples of each type.

Q 15.

Differentiate between globular and fibrous proteins.

Q 16.

Describe the term D- and L-configuration used for amino acids with examples.

Q 17.

Assertion (A): β-glycosidic linkage is present in maltose.
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Reason (R): Maltose is composed of two glucose units in which C-l of one glucose unit is linked to C-4 of another glucose unit.

Q 18.

Classify the following into monosaccharides and disaccharides. Ribose, 2-deoxyribose, maltose, galactose, fructose and lactose.

Q 19.

What are enzymes?

Q 20.

What are the different types of RNA found in the cell?

Q 21.

Which of the following carbohydrates are branched polymer of glucose?
(a) Amylose (b) Amylopectin (c) Cellulose (d) Glycogen

Q 22.

How do you explain the presence of all six carbon atoms in glucose in a straight chain?

Q 23.

α-Helix is a secondary structure of proteins formed by twisting of polypeptide chain into right handed screw like structures. Which type of interactions are responsible for making the a-helix structure stable?

Q 24.

Some enzymes are named after the reaction, where they are used. What name is given to the class of enzymes which catalyse the oxidation of one substrate with simultaneous reduction of another substrate?

Q 25.

Why must vitamin C be supplied regularly in diet?

Q 26.

Structures of glycine and alanine are given below. Show the peptide linkage in glycylalanine.
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Q 27.

Protein found in a biological system with a unique three dimensional structure and biological activity is called a native protein. When a protein in its native form, is subjected to a physical change like change in temperature or a chemical change like, change in pH, denaturation of protein takes place. Explain the cause.

Q 28.

Assertion (A): Glycine must’be taken through diet.
Reason (R): It is an essential amino acid.

Q 29.

What products would be formed when a nucleotide from DNA containing thymine is hydrolysed?

Q 30.

When RNA is hydrolysed, there is no relationship among the quantities of different bases obtained. What does this fact suggest about the structure of RNA?

Q 31.

Why are vitamin A and vitamin C essential to us? Give their important sources.

Q 32.

Proteins can be classified into two types on the basis of their molecular shape, i.e., fibrous proteins and globular proteins. Examples of globular proteins are
(a) insulin (b) keratin (c) albumin (d) myosin

Q 33.

In fibrous proteins, polypeptide chains are held together by
(a) van der Waals forces (b) disulphide linkage
(c) electrostatic forces of attraction (d) hydrogen bonds

Q 34.

Which of the following terms are correct about enzyme?
(a) Proteins (b) Dinucleotides
(c) Nucleic acids (d) Biocatalysts

Q 35.

Match the following enzyme given in Column I with the reactions they catalyse given in Column II.
ncert-exemplar-problems-class-12-chemistry-biomolecules-38

Q 36.

Assertion (A): All naturally occurring a-amino acids except glycine are optically active.
Reason (R): Most naturally occurring amino acids have L-configuration.

Q 37.

Glucose or sucrose are soluble in water but cyclohexane and benzene (simple six membred ring compounds) are insoluble in water Explain.

Q 38.

What are the expected products of hydrolysis of lactose?

Q 39.

Where does the water present in the egg go after boiling the egg?

Q 40.

Why cannot Vitamin C be stored in our body?

Q 41.

What are reducing sugars?

Q 42.

What is the basic structural difference between starch and cellulose?

Q 43.

What type of bonding helps in stabilising the α-helix structure of proteins?

Q 44.

What is the effect of denaturation on the structure of proteins?

Q 45.

Optical rotations of some compounds along with their structures are given below which of them have D configuration.
ncert-exemplar-problems-class-12-chemistry-biomolecules-10

Q 46.

Carbohydrates are classified on the basis of their behaviour on hydrolysis and also as reducing or non-reducing sugar. Sucrose is a .
(a) monosaccharide (b) disaccharide
(c) reducing sugar (d) non-reducing sugar

Q 47.

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Q 48.

Aldopentoses named ribose and 2-deoxyribose are found in nucleic acids.
What is their relative configuration?

Q 49.

How do you explain the presence of an aldehydic group in a glucose molecule?

Q 50.

Match the vitamins given in Column I with the deficiency disease they cause given in Column II.
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