Biology

Biomolecules

Question:

Many organic substances are negatively charged, e.g., acetic acid, while others are positively charged e.g., ammonium ion. An aminoacid under certain conditions would have both positive and negative charges simultaneously in the same molecule. Such a form of aminoacid is called
(a) Positively charged form (b) Negatively charged form
(c) Neutral form (d) Zwitterionic form

Answer:

(d) In aqueous solution, the carboxyl group can lose a proton and amino group can accept a proton, giving rise to a dipolar ion called Zwitter ion. Zwitter ion is neutral but contains both positive and negative charges.

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Biomolecules

Q 1.

Find out how much cellulose is made by all the plants in the biosphere.

Q 2.

How are prosthetic groups different from co-factors?

Q 3.

Can you describe what happens when milk is converted into curd or yoghurt, from your understanding of proteins.

Q 4.

Proteins have primary structure. If you are given a method to know which amino acid is at either of two termini (ends) of a protein, can you connect this information to purity or homogeneity of a protein?

Q 5.

Write the name of any one aminoacid, sugar, nucleotide and fatty acid.

Q 6.

It is said that elemental composition of living organisms and that of inanimate objects (like earth's crust) are similar in the sense that all the major elements are present in both. Then what would be the difference between these two . groups? Choose a correct answer from the following.
(a) Living organisms have more gold in them than inanimate objects
(b) Living organisms have more water in their body than inanimate objects
(c) Living organisms have more carbon, oxygen and hydrogen per unit mass than inanimate objects
(d) Living organisms have more calcium in them than inanimate objects.

Q 7.

Find out and make a list of proteins used as therapeutic agents. Find other applications of proteins.

Q 8.

Formation of enzyme-substrate complex (ES) is the first step in catalysed reactions. Describe the other steps till the formation of product.

Q 9.

Draw the structure of the amino acid, alanine.

Q 10.

What are gums made of ? Is fevicol different ?

Q 11.

Describe the important properties of enzymes.

Q 12.

What are macromolecules ? Give examples.

Q 13.

What is meant by tertiary structure of proteins?

Q 14.

Describe various forms of lipid with a few examples.

Q 15.

Draw the structure of the amino acid, alanine.

Q 16.

Find out a qualitative test for proteins, fats and oils, amino acids and test, any fruit juice, saliva, and urine for them.

Q 17.

Reaction given below is catalysed by oxidoreductase between two substrates A and A’, complete the reaction. A reduced + A‘ oxidised - »

Q 18.

Aminoacids, as the name suggests, have both an amino group and a carboxyl group in their structure. In addition, all naturally occurring aminoacids (those which are found in proteins) are called L-aminoacids. From this, can you guess from which compound can the simplest aminoacid be made?
(a) Formic acid (b) Methane (c) Phenol acid (d) Glycine

Q 19.

The most abundant chemical in living organisms could be
(a) Protein (b) Water (c) Sugar (d) Nucleic acid

Q 20.

Select an appropriate chemical bond among ester bond, glycosidic bond, peptide bond and hydrogen bond and write against each of the following.
a. Polysaccharide
b. Protein
c. Fat
d. Water

Q 21.

Can you attempt building models of biomolecules using commercially available atomic models (Ball and stick models).

Q 22.

Explain the composition of triglycerides. jSfflTriacylglycerols (triglycerides) are the esters of glycerol with fatty acids.

Q 23.

Medicines are either man made (i.e., synthetic) or obtained from living organisms like plants, bacteria, animals etc. and hence the latter are called natural products. Sometimes natural products are chemically altered by man to reduce toxicity or side effects. Write against each of the following whether they were initially obtained as a natural product or as a synthetic chemical.
a. Penicillin
b. Sulfonamide
c. Vitamin C
d. Growth Hormone

Q 24.

What are different classes of enzymes? Explain any two with the type of reaction they catalyse.

Q 25.

Find and write down structures ©f 10 interesting small molecular weight biomolecules.

Q 26.

Attempt titrating an amino acid against a weak base and discover the number of dissociating (ionizable) functional groups in the amino acid.

Q 27.

Illustrate a glycosidic, peptide, and a phospho- diester bond.

Q 28.

Comment on the statement "living state is a non-equilibrium steady state to be able to perform work".

Q 29.

Nucleic acids exhibit secondary structure, justify with example.

Q 30.

Glycine and Alanine are different with respect to one substituent on the a-carbon. What are the other common substituent groups?

Q 31.

Many organic substances are negatively charged, e.g., acetic acid, while others are positively charged e.g., ammonium ion. An aminoacid under certain conditions would have both positive and negative charges simultaneously in the same molecule. Such a form of aminoacid is called
(a) Positively charged form (b) Negatively charged form
(c) Neutral form (d) Zwitterionic form

Q 32.

Starch, Cellulose, Glycogen, Chitin are polysaccharides found among the following. Choose the one appropriate and write against each.
Cotton fibre __________
Exoskeleton of Cockroach __________
Liver __________
Peeled potato __________

Q 33.

Nucleic acids exhibit secondary structure. Describe through Watson-Crick Model.

Q 34.

What is the difference between a nucleotide and nucleoside? Give two examples of each with their structure.