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#	Question	Answer
1	What is observed when elemental analysis is performed on living tissues?	Elements like carbon, hydrogen, oxygen and several others are found in living tissues.
2	What remains after a tissue is fully burnt?	Ash containing inorganic elements and compounds.
3	What are amino acids?	Organic compounds containing an amino group and an acidic group attached to the same carbon (alpha-carbon).
4	Which amino acid has a methyl group as its R group?	Alanine.
5	Name the aromatic amino acids mentioned in the text.	Tyrosine, phenylalanine and tryptophan.
6	Are lipids generally water soluble or insoluble?	Lipids are generally water insoluble.
7	What are saturated fatty acids?	Fatty acids without double bonds.
8	On what basis are fats and oils differentiated?	Melting point.
9	Which tissues contain lipids with more complex structures?	Neural tissues.
10	Name all the nucleotides mentioned in the text.	Adenylic acid, thymidylic acid, guanylic acid, uridylic acid and cytidylic acid.
11	In which organisms are secondary metabolites commonly found?	Plant, fungal and microbial cells.
12	Which four classes of organic compounds are present in the acid-insoluble fraction?	Proteins, nucleic acids, polysaccharides and lipids.
13	What does the acid-soluble pool roughly represent?	Cytoplasmic composition.
14	What percentage of cellular mass is carbohydrates?	3%.
15	How are amino acids linked in proteins?	By peptide bonds.
16	Which protein is the most abundant in the animal world?	Collagen.
17	Why is cellulose called a homopolymer?	Because it consists of only one type of monosaccharide, glucose.
18	In a polysaccharide chain, which end is called the non-reducing end?	The left end.
19	What is chitin?	A complex polysaccharide present in the exoskeleton of arthropods.
20	Which nitrogenous bases are pyrimidines?	Cytosine, uracil and thymine.
21	Which amino acid is called the N-terminal amino acid?	The first amino acid in a protein chain.
22	Why is tertiary structure important in proteins?	It is absolutely necessary for many biological activities of proteins.
23	What is the primary structure of an enzyme?	The amino acid sequence of the protein.
24	What is a physical change?	A change in shape or state without breaking chemical bonds.
25	How do catalysed reactions compare with uncatalysed reactions?	Catalysed reactions proceed at much higher rates.
26	How many enzyme-catalysed reactions convert glucose into pyruvic acid?	Ten different reactions.
27	Where does the substrate bind on the enzyme?	At the active site within a cleft or pocket.
28	What does the x-axis represent in the activation energy graph?	Progression of structural transformation through the transition state.
29	What happens after the ES complex forms?	It dissociates into product(s) and unchanged enzyme through enzyme-product (EP) complex.
30	Which factors can alter the tertiary structure of enzymes?	Temperature, pH, substrate concentration and binding of specific chemicals.
31	What effect does low temperature have on enzymes?	It preserves enzymes in a temporarily inactive state.
32	What is inhibition?	The process in which binding of a chemical shuts off enzyme activity.
33	Which substrate does malonate resemble structurally?	Succinate.
34	What are hydrolases?	Enzymes catalysing hydrolysis of ester, ether, peptide and other bonds.
35	What is an apoenzyme?	The protein portion of an enzyme.
36	What are co-enzymes?	Organic compounds loosely associated with apoenzymes during catalysis.
37	Which metal ion acts as a cofactor for carboxypeptidase?	Zinc.
38	How many types of amino acids are present in living organisms?	20 types.
39	Why are lipids found in the macromolecular fraction?	Due to their association with membranes.
40	What is the function of nucleic acids?	They serve as genetic material.
41	Which protein is the most abundant in the biosphere?	Ribulose bisphosphate Carboxylase-Oxygenase (RuBisCO).
42	What is the function of nucleic acids in heredity?	They carry hereditary information from parents to progeny.