Biomolecules

Benedict's solution

Iodine solution

Fehling's solution

Schiff's reagent

Starch

Glycogen

Cellulose

Amylose

Fructose

Galactose

Glucose

Ribose

$\alpha$-1,4-glycosidic linkage

$\beta$-1,4-glycosidic linkage

$\alpha$-1,6-glycosidic linkage

$\beta$-1,6-glycosidic linkage

1 and 2

3 and 4

1 and 4

2 and 3

C-1 of glucose and C-2 of fructose

C-1 of glucose and C-4 of fructose

C-1 of glucose and C-1 of fructose

C-2 of glucose and C-2 of fructose

It is an aldose

It is a hexose

It is a non-reducing sugar

It shows mutarotation

An aldehyde group

A ketone group

A carbonyl group

A primary alcohol group

4

8

16

2

$C1$ and $C6$

$C1$ and $C4$

$C1$ and $C2$

$C1$ and $C1$

Alanine

Methionine

Cysteine

Serine

The peptide bonds remain intact

The peptide bonds are broken

New peptide bonds are formed

The primary structure is preserved

Carbohydrates

Vitamins

Proteins

Lipids

10

20

50

100

It remains stationary at the origin because the molecule exists as a neutral zwitterion at this $pH$.

It migrates toward the cathode because at $pH$ 7.4, the amino acid exists primarily in its cationic form.

It migrates toward the anode because at $pH$ 7.4, the amino acid exists primarily in its anionic form.

It migrates toward the cathode because at $pH$ 7.4, the amino acid exists primarily in its anionic form.

Arginine

Asparagine

Lysine

Histidine

Their large molecular weight

The presence of peptide bonds

The formation of Zwitterions

The existence of $L$-configuration

Protect the amino group

Protect the carboxyl group

Activate the carboxyl group for amide bond formation

Sequence the amino acids

Cysteine

Cystine

Methionine

Serine

Gly-Ala-Phe

Phe-Gly-Ala

Ala-Gly-Phe

Ala-Phe-Gly

Pressure and volume

Temperature and pH

Color and density

Mass and weight

Lipids

Proteins

Carbohydrates

Nucleic acids

Maltase

Sucrase

Lactase

Cellulase

Opposite charges

Complementary shapes

Identical structures

Variable shapes

Hydrolases

Isomerases

Lyases

Ligases

It is always a strong permanent covalent bond

It typically involves weak interactions like hydrogen bonding or Van der Waals forces

It is a metallic bond

No chemical interaction occurs until the product is formed

The maximum speed of the reaction

The concentration of the enzyme

The affinity of the enzyme for its substrate

The temperature sensitivity of the enzyme

Most coenzymes are derivatives of vitamins.

Coenzymes serve as transient carriers of specific functional groups.

A single coenzyme can work with many different apoenzymes.

Coenzymes are always made up of long chains of amino acids.

Transferases

Lyases

Isomerases

Hydrolases

A stable intermediate with the lowest energy level.

A short-lived, high-energy molecular configuration where bonds are being broken and formed.

The state where the enzyme is completely denatured.

The final state where the product is released from the active site.

Vitamin B12

Vitamin A

Vitamin C

Vitamin D

Vitamin B1

Vitamin C

Vitamin A

Vitamin B6

Vitamin B2

Vitamin K

Vitamin A

Vitamin E

Vitamin A

Vitamin D

Vitamin C

Vitamin K

Vitamin A

Vitamin C

Vitamin K

Vitamin E

Vitamin $B_{1}$

Vitamin C

Vitamin E

Vitamin K

Pantothenic acid ($B_{5}$)

Ascorbic acid

Calciferol

Retinol

1 mg Niacin from 10 mg Tryptophan

1 mg Niacin from 60 mg Tryptophan

10 mg Niacin from 1 mg Tryptophan

60 mg Niacin from 1 mg Tryptophan

They are chemically more reactive than water-soluble vitamins.

They are not excreted in the urine and accumulate in the liver and adipose tissues.

They catalyze the breakdown of essential water-soluble vitamins.

They increase the acidity of the blood significantly.

Two

Three

Four

Six

Sugar and Base

Base and Phosphate

Sugar and Phosphate

Base and Base

Phosphate

Ribose

Adenine

Cytosine

Deoxyribonucleoside

Ribonucleotide

Deoxyribonucleotide

Ribonucleoside

Ribose

2-Deoxyribose

Glucose

Galactose

Oxygen is missing at the $C_{2}$ position of the ribose ring.

The sugar has only two oxygen atoms in total.

There are two deoxy groups at $C_{1}$ and $C_{2}$.

The ring is a 2-membered ring.

Adenine

Guanine

Uracil

None of the above

It involves the formation of new phosphodiester bonds by the enzyme DNA polymerase.

It results in two identical DNA molecules, each containing two completely new strands.

It occurs in the $3' \rightarrow 5'$ direction only.

It breaks the covalent bonds between the sugar and the base.

DNA is single-stranded.

DNA contains Uracil which is more stable than Thymine.

The absence of the $2'-OH$ group in DNA makes it less reactive towards hydrolysis.

DNA can replicate itself without enzymes.

Erwin Chargaff

Rosalind Franklin

Linus Pauling

Frederick Griffith

Ribose has an -OH group at $C2'$ while Deoxyribose has -H at $C2'$.

Deoxyribose has an -OH group at $C3'$ while Ribose has -H at $C3'$.

Ribose is a hexose, Deoxyribose is a pentose.

Deoxyribose has an extra oxygen at $C5'$.

Melatonin

Thyroxine

Insulin

Oxytocin

They are recycled by the gland

They are inactivated and excreted

They are stored in the liver

They become vitamins

Pituitary gland

Adrenal gland

Thyroid gland

Pancreas

Estrogen

Progesterone

Testosterone

Insulin

Increasing the excretion of water

Causing vasoconstriction of blood vessels

Lowering the heart rate

Dilating the arteries to the skin

Cerebellum

Hypothalamus

Medulla oblongata

Pons

Two six-membered rings

Three six-membered and one five-membered ring

Four six-membered rings

Two six-membered and two five-membered rings

High blood glucose

Low pH (acidity) in the duodenum

High fat content in the diet

Low blood calcium levels

$Na^{+}$

$K^{+}$

$Ca^{2+}$

$Mg^{2+}$

Insulin

Adrenaline

Thyroxine

Glucagon

Solubility increases

Solubility decreases (they often coagulate)

Solubility remains exactly the same

Solubility becomes infinite

It is present in all proteins

It involves the arrangement of multiple polypeptide chains

It is only stabilized by peptide bonds

It describes the sequence of amino acids

Spherical

Thread-like or fiber-like

Irregular clumps

Cubic

Strong acids

Heavy metal salts

Distilled water at room temperature

Concentrated urea

The names of the two different polypeptide subunits of a dimeric protein like insulin.

The specific side chains or R-groups that determine the protein's solubility.

The free amino group ($-NH_2$) and the free carboxyl group ($-COOH$) at the opposite ends of the chain.

The two specific locations where the chain undergoes denaturation during heating.

In an $\alpha$-helix, the hydrogen bonds are intramolecular, whereas in a $\beta$-pleated sheet, they are intermolecular.

In an $\alpha$-helix, the hydrogen bonds are intermolecular, whereas in a $\beta$-pleated sheet, they are intramolecular.

Both $\alpha$-helix and $\beta$-pleated sheets are stabilized primarily by ionic interactions and disulfide bridges.

The $\alpha$-helix is a planar sheet-like structure, while the $\beta$-pleated sheet is a coiled right-handed screw.

Primary

Secondary

Tertiary

Pentary

The protein molecules become smaller and less heavy.

Hydrophobic groups previously buried in the interior are exposed, leading to aggregation.

The protein molecules acquire a large net charge.

The peptide bonds are converted into ether linkages.

Frying an egg.

Adding a small amount of salt to a protein solution (salting out/in) without extreme pH/heat.

Curdling of milk with acid.

Permanent waving of hair using reducing and oxidizing agents (though technically a chemical modification of crosslinks).

The planar nature of the peptide bond and the tetrahedral geometry of the $\alpha$-carbon.

The presence of bulky proline residues at every turn.

The repulsion between carbonyl oxygens.

The formation of disulfide bridges at regular intervals.