Q1​)Describe the molecular composition of carbohydrates,protein,Fat, and Nucliec acid?

Answer:- ​Carbohydrates​ consist of carbon,hydrogen and oxygen with a ratio of hydrogen

twice that of carbon and hydrogen . Carbohydrate include sugars,starches,cellulose and
many other compounds found in living organisms . In their basic form carbohydrates are
simple sugars or mononsacchride . These simple sugar combine with each other to form
more complex carbohydrates . The composition of two simple sugars is disacchride .
Carbohydrates consist of two to ten simple sugars are called oligonsacchride and those with
a large number are called polysacchride.
Protein​ are large organic molecules containing the elements , carbon , hydrogen , oxygen ,
nitrogen , and sulphur . One mole of protein produces 4000 calories of energy. Their main
role is in building material in the body. They help in growth and repair of body parts. They
make structure like muscles nail and hair. They make red blood cells which contain
haemoglobin for the transport of oxygen in our body. They make enzymes. They are broken
down in our body into amino acids,from these our cells make their own type of protein. They
are also the building material of protoplasm and membrane system.
Fat​ ​ acid are include in the group of derived lipids . It is the most common component of
lipids in the body . They are generally found in the ester bond linkage in different classes of
lipids . In the human body free fatty acid are formed only during metabolism . Fatty acid are
aliphatic carboxylic acid and have the general formula R-CO-OH where COO (carboxylic
acid ) represents the functional group depending upon the R group (the hydrocarbon chain) .
Nucliec​ a ​ cid​ are the biopolymers of small biomolecules essential for all known forms of life
. The term nucleic acid is the overall name for DNA and RNA . They are composed of
nucleotides , which are the monomers of three components a five carbon sugar , a
phosphate group , and a nitrogenous base.

Q2​)Define metabolism , Anabolism and catabolism?

Answer:​-​Metabolism​ The process that occur within a living organisms in order to maintain
life.
Anabolism​ The synthesis of complex molecules in living organisms from simpler ones
together with the storage of energy; constructive metabolism.
Catabolism​ The breakdown of complex molecule in living organism to form simple ones ,
together with the release of energy , destructive metabolism.

Q3​)Define ATP and discuss its relationship with catabolism and anabolism?
Answer:-​ATP​ Adenosine triphosphate is the energy currency of life . ATP is high energy
molecule found in every cell . Its job is to store eneergy and supply the cell with needed
energy.

Anabolism and Catabolism are interrelated with each other through the molecule ATP . The
high energy phosphate bond of ATP store energy captured in catabolism and later release in
anabolic reaction . Catabolic reaction break large molecule , releasing energy which is used
to form ATP.

Q4​)Define the following terms Glycogenesis,Transamination,Deamination, and Ketosis ?

Answer:​-Glycogenesis​ The formation of glycogen from sugar or from molecule of glucose.
Glycogenlysis​ is the breakdown of the molecule glycogen to glucose , a simple sugar that
the uses to produce energy.
Transamination​ is a reversible reaction in which α-NH2 group of one amino acid is
transferred to a α-ketoacid resulting in formation of a new amino acid and a new ketoacid.
Deamination​ is the process by which N– of amino acid is removed as NH3.
Ketosis​ Accumulation of abnormal amount of ketone bodies in tissues and body fluids is
termed as ketosis, where the urinary excretion of β-OH butyric acid exceeds 200 mg daily
(normal 5 to 10 mg). The overall pattern is called ketosis.

Q5​)Define carbohydrates . Explain the classification of carbohydrates ?

Answers:​-​Definition​: Carbohydrates are defined chemically as aldehyde or ketone
derivatives of the higher polyhydric alcohols, or compounds which yield these derivatives on
hydrolysis.
Carbohydrates are divided into four major groups—monosaccharides, disaccharides,
oligosaccharides and polysaccharides.
1. Monosaccharides​: (also called ‘simple’ sugars) are those which cannot be hydrolysed
further into simpler forms.
General formula : CnH2nOn
They can be subdivided further:
(a) Depending upon the number of carbon atoms they possess, as trioses, tetroses,
pentoses, hexoses, etc.
(b) Depending upon whether aldehyde (– CHO) or ketone (– CO) groups are present as
aldoses or ketoses.
2. Disaccharides​: Those sugars which yield two molecules of the same or different
molecules of monosaccharide on hydrolysis.
General formula : Cn(H2O)n-1
Examples
• Maltose yields 2 molecules of glucose on hydrolysis.
• Lactose yields one molecule of glucose and one
molecule of galactose on hydrolysis.
• Sucrose yields one molecule of glucose and one
molecule of fructose on hydrolysis.
• Lactulose a keto disaccharide
3. Oligosaccharides​: Those sugars which yield 3 to 10 monosaccharide units on
hydrolysis, e.g. Maltotriose.
4. Polysaccharides​ (Glycans): Those sugars which yield
more than ten molecules of monosaccharides on hydro-
lysis.
General formula: (C6H10O5)n
Polysaccharides are further divided into two groups:
a. Homopolysaccharides (homoglycans): Polymer of same monosaccharide units.
Examples—Starch, glycogen, inulin, cellulose,
dextrins, dextrans.
b. Heteropolysaccharides (heteroglycans): Polymer of different monosaccharide units or
their derivatives.
Example—Mucopolysaccharides (glycosamino-
glycans).

Q6​)Discuss the general structure of amino acids ?

Answer:​-​Amino acid​ are molecules used to build proteins . All amino acids have a central
carbon atom surrounded bya hydrogen atom , a carboxyl group (COOH) , an amino group
(NH2) and an R group . It is the R group or side chain that differs the 20 amino acids. Some
amino acids such as glycine and cysteine are used as detoxicants of specific substances.
Cystine and methionine are sources of sulphur.
New Amino Acids
In addition to 20 L-amino acids that take part in protein synthesis, recently two more new
amino acids described. They are:
A. Selenocysteine - 21st amino acids
Selenocysteine is recently introduced as 21st amino acid.Selenocysteine occurs at the
“active site” of severalenzymes.
Examples include:
• Thioredoxin reductase
• Glutathione peroxidase which scavenges peroxides,
• De-iodinase that converts thyroxine to triiodothyronine
• Glycine reductase
• Selenoprotein P, a glycoprotein containing 10
selenocysteine residues, found in mammalian blood.It has an antioxidant function and its
concentrationfalls in selenium deficiency.
B. Pyrrolysine - 22nd amino acid
Recently it has been claimed as 22nd amino acid by some scientists. The STOP codon UAG
can code for pyrrolysine.

Q7​)Discuss the following

a)Essential and non essential
b)Polar and non polar
c)Zwitter ion
Answer:-​a)Essential amino acids​ are the amino
acids which are not synthesized by the body and must be taken in the diet.They include:
MATT VIL PHL
Methionine, Arginine, Threonine,
Tryptophan, Valine, Isoleucine, Leucine,
Phenylalanine, Histidine, Lysine.
Non essential amino acids​ are those
amino acids which are synthesized by the
body and need not to be taken in the
diet.
AAACGGG PST
Alanine,Asparagine,Aspartic acid,Cysteine,Glutamic
acid,Glutamine,Glycine,Proline,Serine,Tyrosine
b)Polar amino acid​ Amino acid with ionizable side chain are polar example
valine,proline,serine, etc.
Non polar amino acid​ Amino acid with non ionizable side chain are non polar example
cysteine,glycine,methionine etc.
There are some of the structures of nonpolar reminder acid
Polar amino acid with no charge
These amino acids do not have any charge on the R group. These amino acids participate in
hydrogen bonding of protein structure. The amino acids in this group are serine , threonine ,
tyrosine, cysteine, glutamine and aspargine.

Polar amino acid with positive charge

Polar amino acids with positive charge have more amino groups as compared to carboxyl
groups making 8 basic. The amino acids which have positive charge on the R group are
placed in this category. They are lysine , arginine and histidine.

​ olar amino acids with negative charge

P
Polar amino acids with negative charge have more carboxyl groups making them acidic. The
amino acids which have negative charge on R group are placed in this categoty. They are
called as dicarboxylic mono amino acids. They are aspartic acid and glutamic acid.

c)Zwitter ions or dipolar ions​: amino acids

having equal no. of positive and negative
charges.
Q8​)Describe the Classification of protein according to solubility,composition,function, and
shape ?
Answer:-​Protein classification based on solubility
The different globular proteins can be classified based on their solubility in different solvents,
such as water, salt and alcohol
Protein classification based on chemical composition
On the basis of their chemical composition, proteins may be divided into two classes: simple
and complex.
Simple proteins
Also known as homoproteins, they are made up of only amino acids. Examples are plasma
albumin, collagen, and keratin.
Conjugated proteins
Sometimes also called heteroproteinas, they contain in their structure a non-protein portion.
Three examples are glycoproteins, chromoproteins, and phosphoproteins.
Protein classification based on biological functions
The multitude of functions that proteins perform is the consequence of both the folding of the
polypeptide chain, therefore of their three-dimensional structure, and the presence of many
different functional groups in the amino acid side chains, such as thiols, alcohols, thioethers,
carboxamides, carboxylic acids and different basic groups.
From the functional point of view, they may be divided into several groups.
1)Enzymes
2)Transport proteins
3)Storage proteins
4)Mechanical support
5)They generate movement
6)They are involved in nerve transmission.
7)Hormones
8)Protection against harmful agents.
9)Storage of energy.
Protein classification based on shape
On the basis of their shape, proteins may be divided into two classes: fibrous and globular.

Q9​)Describe Primary,Secondary,Tertiary and quaternary structure of protein ?

Answer:​(a) Primary structure​:Primary structure is the linear sequence of amino acids
held together by peptide bonds in its peptide chain. The peptide bonds form the backbone
and side chains of amino acid residues project outside the peptide backbone. The free -NH2
group of the terminal
amino acid is called as N-terminal end and the free -COOH end is called as C-terminal end.
It is a tradition to number the amino acids from N-terminal end as No. 1 towards the
C-terminal end. Presence of specific amino acids at a specific number is very significant for a
particular function of a protein. Any change in the sequence is abnormal and may affect the
function and properties of protein.
Secondary Structure​: The peptide chain thus formed assumes a three dimensional
secondary structure by way of folding or coiling consisting of a helically-coiled, zig- zag,
linear or mixed form. It results from the steric relationship between amino acids located
relatively near each other in the peptide chain. The linkages or bonds involved in the
secondary structure formation are hydrogen bonds and disulfide bonds.
Tertiary structure​: The polypeptide chain with
secondary structure mentioned above may be further folded, superfolded twisted about itself
forming many sizes. Such a structural conformation is called tertiary structure. It is only one
such conformation which is biologically active and protein in this conformation is called as
native protein. Thus the tertiary structure is constituted by steric relationship between the
amino acids located far apart but brought closer by folding.
Quaternary Structure​: Many proteins are made up of only one peptide chain. However,
when a protein consists of two or more peptide chains held together by non-covalent
interactions or by covalent cross-links, it is referred to as the quaternary structure. The
assembly is often called as oligomer and each constituent peptide chain is called as
monomer or subunit. The monomers of
oligomeric protein can be identical or quite different in primary, secondary or tertiary
structure.

Q10​)Discuss isomerism with at least two examples?

Answer:​-Isomerism ​It is a phenomenon where two or more compounds have the
same chemical formula but possess different structural formulas , that is , different
properties . This is mainly because of different structure or spatial arrangement .

Example 1)D-glucose and L-glucose

2)Butane and isobutane

Q11​)Discuss acid , base and redox reaction ?

Answer:​Acid
A substance that becomes ionized when placed in solution, producing positively charged
hydrogen ions, H+. An acid is considered a proton donor.
(Remember, atoms always have the same number of electrons as protons. Ions are
produced when an atom gains or loses electrons.)
Base
A substance that becomes ionized when placed in solution, producing negatively charged
hydroxide ions, (OH)–. Bases are referred to as being more alkaline than acids and are
known as proton acceptors.
Redox Reaction
• Redox (reduction-oxidation) reactions include
all chemical reactions in which atoms have
their oxidation state changed by either gaining
electrons (reduction) or losing electrons
(oxidation). Substances that have the ability to
oxidize other substances are said to be oxidative and are known as oxidizing agents,
oxidants or oxidizers. An oxidant removes electrons from another substance.
Similarly, substances that have the ability to reduce other substances are said to be
reductive and are known as reducing agents, reductants, or reducers.