Biomolecules, Dyes and Spectral Techniques

Amino acids: Classification, structure and stereochemistry, acid base behaviour, isoelectric point, electrophoresis, preparation and reactions of α-amino acids.

Proteins: Peptide linkages, structure and classification of primary, secondary and tertiary proteins and denaturation.

Nucleic acids:  Introduction, protein synthesis, functions.

Self Study: Structure of nucleic acids, ribonucleosides and ribonucleotides, double helical structure of DNA.

Classification and nomenclature, monosaccharides, mechanism of osazone formation, interconversion of glucose and fructose, chain lengthening and chain shortening of aldoses, configuration of monosaccharides, erythro and threodiastereomers, conversion of glucose into mannose. formation of glycosides, ethers and esters, determination of ring size of monosaccharides, cyclic structure of D-(+)-glucose , mechanism of mutarotation.

Colour and constitution (electronic concept), classification of dyes, chemistry and synthesis of methyl orange, congo red, malachite green, crystal violet, phenolphthalein, fluorescein, alizarin and indigo.

Electromagnetic radiation, quantization of energy, regions of electromagnetic spectrum,

Lambert – Beer law, molar absorptivity, different electronic transitions and symmetry rules, effect of solvent on transitions, effect of conjugation, concept of chromophores and auxochromes, bathochromic, hypsochromic, hyperchromic and hypochromic shift. Woodward Fieser rules and its applications on enes, dienes, α,β-unsaturated carbonyls and extended conjugations.

Molecular vibrations, Hooke’s law, different regions of IR spectrum (finger print and functional group region), selection rules, characteristic intensity and position of IR bands of various functional groups (alkanes, alkenes, alkyl halides, alcohols, ethers, carbonyl compounds, primary and secondary amines, carboxylic acids and its derivatives); effect of solvent and hydrogen bonding.