1. PARTII_Protein
1.1. Features
1.1.1. More than 100 aminoacid
1.1.2. Peptide linkage
1.1.3. Polypeptides
1.1.4. N,S, C,H, O elements in protein
1.2. Classification
1.2.1. Chemical Composition
1.2.1.1. Simple
1.2.1.1.1. Features
1.2.1.1.2. Example
1.2.1.2. Conjugated
1.2.1.2.1. Features
1.2.1.2.2. Example
1.2.2. Function
1.2.3. Shape
1.2.3.1. Fibrous
1.2.3.1.1. Features
1.2.3.1.2. Example
1.2.3.2. Globular
1.2.3.2.1. Features
1.2.3.2.2. Example
1.3. Structure
1.3.1. Primary
1.3.1.1. Features
1.3.1.1.1. - S - S - Bond
1.3.1.1.2. Covalent bond With aminoacid sequence
1.3.2. Secondary
1.3.2.1. Features
1.3.2.1.1. Refers Shape of Long-chain aminoacid
1.3.2.1.2. H-bond
1.3.2.2. Parts (Any 1 or 2 exist)
1.3.2.2.1. Alpha-helix
1.3.2.2.2. Pleaded sheet
1.3.2.2.3. Random coil
1.3.3. Tertiary
1.3.3.1. Features
1.3.3.1.1. 3D-Conformation Of protein
1.3.3.2. Parts
1.3.3.2.1. Alpha-helix
1.3.3.2.2. Pleaded sheet
1.3.3.2.3. Random coil
1.3.4. Quarternary
1.3.4.1. Features
1.3.4.1.1. Complex protein
1.3.4.1.2. Complete Protein
1.3.4.1.3. 2 or more peptide chain
1.3.4.2. Example
1.3.4.2.1. Haemoglobin
2. PART1_Aminoacid
2.1. Aminoacid
2.1.1. Synthesis
2.1.1.1. Strecker
2.1.1.2. Gabriel Phthalimide
2.1.2. Reactions
2.1.2.1. Esterfication
2.1.2.2. -NH2 Acetylation
2.1.2.3. Cu2+ Complexation
2.1.3. Ninhydrin Test
2.1.3.1. Features
2.1.3.1.1. Ninhydrin + Protein gives Violet color
2.1.3.1.2. Test for alpha-aminoacid, Protein, Dipeptide
2.1.4. Zwitterion
2.1.4.1. Features
2.1.4.1.1. Dipolar nature Of Aminoacid In aqueous solution
2.1.4.1.2. Neutral/ Net charge =0
2.1.5. Amphoteric i.e., readily react with acids or bases
2.1.6. Isoelectric point
2.1.6.1. Features
2.1.6.1.1. pH =7
2.1.6.1.2. Water soluble
2.1.6.1.3. pH point at which Aminoacid completely Exist as Zwitterion
3. PARTIII_PEPTIDES
3.1. Features
3.1.1. Elimination of H2O from two aminoacid forms Dipeptide
3.1.2. Peptide linkage -C=O I -N-H
3.2. Edmann Degradation
3.2.1. Sequencing Peptides from N-terminus
3.2.1.1. How !!
3.2.1.1.1. 3) Shortened peptide chain & Phenylthiohydantoin as products
3.2.1.1.2. 1) Treating peptide with phenyl isothiocyanate
3.2.1.1.3. 2) Acid hydrolysis
3.2.1.2. Features
3.2.1.2.1. No interruptions On sequencing frm N-terminus
3.3. Terminal Analysis
3.3.1. C-Terminus
3.3.1.1. Carboxypeptidase
3.3.1.1.1. Types
3.3.1.2. Thiohydantoin
3.3.2. N-terminus
3.3.2.1. Sanger reagent_ _DNF
3.3.2.2. Dansyl chloride
3.3.2.3. Edmann Degradation_ _PITC
3.4. Dipeptide Synthesis
3.4.1. Bergmann Method
3.4.2. Phthaloyl chloride
3.4.3. Merrified resin method