(i) The amino acids are linked covalently by peptide bonds. The carboxyl group of the first amino acid react with the amino group of the second amino acid to give an amide linkage between these amino acids. This amide linkage is called peptide bond. The resulting compound is called a dipeptide. Addition an another amino acid to this dipeptide a second peptide bond results in tripeptide.

(ii) Thus we can generate tetra peptide, penta peptide etc... When you have more number of amino acids linked this way you get a polypeptide. If the number of amino acids are less it is called as a polypeptide, if it has large number of amino acids (and preferably has a function) then it is called a protein.
(iii) The amino end of the peptide is known as N - terminal or amino terminal while the carboxy end is called C-terminal or carboxy terminal. In general protein sequences are written from N-Terminal to C-Terminal.The atoms other than the side chains (R-groups) are called main chain or the back bone of the polypeptide.

Primary structure of Proteins:
Proteins are polypeptide chains, made up of amino acids are connected through peptide bonds. The relative arrangement of the amino acids in the polypeptide chain is called the primary structure of the protein. Knowledge of this is essential as even small changes have potential to alter the overall structure and function of a protein.
\(\mathrm{H}_{2} \mathrm{~N}-\mathrm{Gly}-\mathrm{Met}-\mathrm{Phe}-\mathrm{Cys}-\mathrm{Arg}-\mathrm{Asp}-\mathrm{COOH}\)
α - Helix:
In the α-helix sub-structure, the amino acids are arranged in a right handed helical (spiral) structure and are stabilised by the hydrogen bond between the carbonyl oxygen of one amino acid (n residue) with amino hydrogen of the fifth residue (n + 4^th residue). The side chains of the residues protrude outside of the helix. Each turn of an α-helix contains about 3.6 residues and is about 5.4 Å long. The amino acid proline produces a kink in the helical structure and often called as a helix breaker due to its rigid cyclic structure.

1. Linear sequence of aminoacids
2. Linear
3. Composed of peptide bonds formed between amino acids.
Secondary structure of Proteins:
The amino acids in the polypeptide chain forms highly regular shapes (sub-structures) through the hydrogen bond between the carbonyl oxygen (-C=O) and the neighbouring amine hydrogen (-NH) of the main chain. α-Helix and β-strands or sheets are two most common substructures formed by proteins.

β-Strand:
β-Strands are extended peptide chain rather than coiled. The hydrogen bonds occur between main chain carbonyl group one such strand and the amino group of the adjacent strand resulting in the formation of a sheet like structure. This arrangement is called β-sheets.

i) Reducing sugars:
1. Sugars which reduce Tollen's reagent or Fehling's solution or Benedict's solution are called reducing sugars.
2. These contain either α - hydroxyl ketone or cyclical hemi acetal or hemi ketal or structures in equilibrium with open chain forms having a free- CHO or C=O group.
3. E.g. a) All monosaccharide's like D - glucose, D - fructose (aldoses and ketoses)
b) Sugars like Lactose and maltose except sucrose.
ii) Non - reducing sugars:
1. Sugars which do not reduce either Tollen's reagent, Fehling's solution or Benedict's solution are called non-reducing sugars.
2. They contain a stable acetal or ketal structures which cannot be opened into a free carbonyl group.
E.g. Sucrose, starch, cellulose, glycogen, dextrin etc.