All questions of Biomolecules for NEET Exam
In DNA the complimentary base are
Adenine and thymine.
Guanine and cytosine
The genetic information for cell is contained
in the sequence of bases A, T, G and C in
DNA molecule.
The DNA sequence that codes for a specific
protein is called a Gene and thus every
protein in a cell has a corrosponding gene.
Sucrose does not have free — CHO or
CO group, hence it does not undergo
mutarotation.
Cell membranes (Plasma membranes) constitutes bilayer of phospholipid with embedded proteins. In humans, lipids accounts for upto 79% of cell membrance.
Amount of A = T and that of G = C.
Thyroxine is an amino hormone.
Phospholipids are derivatives of glycerol in
which two of the hydroxyl groups are
esterified with fatty acids while the third is
esterified with some derivative of phosphoric
acid with some alcohol such as choline,
ethanolamine, serine or inositol.
Triglycerides are lipids, hence these are
hydrolysed by lipases to glycerol and fatty
acids.
Haemoglobin acts as an oxygen carrier in
the blood since it reacts with oxygen to form
unstable oxyhaemoglobin which easily
breaks to give back haemoglobin and
oxygen.
We know that cellulose (C6H12O6 )n is the
chief constituent of cell walls of plants. It is
the most abundant organic substance found
in nature. It is a polymer of glucose with
3500 repeat units in a chain.
Each nucleic acid consists of a pentose
sugar a heterocyclic base, and phosphoric
acid. The sugar present in DNA is 2-deoxy
-D (–) ribose and the sugar present in RNA
is D (–)- ribose. The chirality of DNA and
RNA molecules are due to the presence of
sugar components.
The α-helix structure is formed when the
chain of α-amino acids coils as a right
handed screw (called α-helix) because of the
formation of hydrogen bonds between
amide groups of the same peptide chain, i.e.,
NH group in one unit is linked to carbonyl
oxygen of the third unit by hydrogen
bonding. This hydrogen bonding between
different units is responsible for holding
helix in a position.
When the proteins are subjected to the
action of heat, mineral acids or alkali, the
water soluble form of globular protein
changes to water insoluble fibrous protein.
This is called denaturation of proteins.
During denaturation secondary and tertiary
structures of protein destroyed but primary
structures remains intact.
The bond formed between two amino acids
by the elimination of a water molecule is
called a peptide linkage or bond. The peptide
bond is simply another name for amide bond.
The product formed by linking amino acid
molecules through peptide linkages. —
CO—NH—, is called a peptide
All proteins are not found in L-form but they
may be present in form of D or L
Testorterone and Adrenaline are steroid
harmone, Thyroxin is non-steroided harmone
glucagon is peptide harmone.
Enzymes are most reactive at optimum
temperature. The optimum temperature for
enzyme activity lies between 40°C to 60°C.
It is a common pathway for both the aerobic
& anaerobic respiration in which 1 glucose
molecule is converted to 2 molecules of
pyruvate.
The base pairs of the two strands of DNA
are linked together through H-bonds.
Thiol group participates in disulphide bond formation in proteins
Disulphide bonds play a crucial role in stabilizing the tertiary structure of proteins by covalently linking different parts of the polypeptide chain. The formation of disulphide bonds involves the oxidation of two thiol groups (-SH) to form a covalent bond between the sulfur atoms.
Thiol group
- Thiol group, also known as sulfhydryl group, is a functional group containing a sulfur atom bonded to a hydrogen atom.
- In proteins, cysteine residues contain thiol groups that can participate in disulphide bond formation.
Disulphide bond formation
- The process of disulphide bond formation involves the oxidation of two thiol groups to form a covalent bond between the sulfur atoms.
- This process is often catalyzed by enzymes known as disulphide bond isomerases.
Importance of disulphide bonds
- Disulphide bonds play a crucial role in stabilizing the tertiary structure of proteins.
- They can help maintain the structural integrity of proteins in various environments.
In conclusion, the thiol group participates in disulphide bond formation in proteins by undergoing oxidation to form covalent bonds between sulfur atoms. This process is essential for maintaining the structural stability of proteins.
Thyroxine is the only hormone among the
given choices that contains iodine. Its
structure is as follows:
Fructose which is another form of starch.
having an aldehydic group which reacts with Fehlingsoln and reduces it.
Insulin helps in converting glucose to
glycogen
Pepsin and Trypsin are two enzymes
involved in the process (hydrolysis of
proteins)
Sucrose is a disaccharide of α–DGlucopyranose
and β–D-Fructofuranose.
Enzymes are made up of protein with specific
structure.
Vitamins are organic substances which does
not provide energy but are essential for
healthy growth and proper functioning of
body. Vitamins are not synthesized inside
human body but they are essential part of
our diet.