Clear your doubts on Biochemistry with Kings FMGE coaching classes
Attention Foreign Medical Graduates! If you’re aiming to excel in the upcoming FMG exam within a tight timeframe of 2 months, don’t fret! We’ve got you covered. With our expert guidance at Kings FMGE Coaching, you can confidently ace the FMGE in just two months. In this blog post, we will delve into the subject of Biochemistry, specifically focusing on the topic of “Proteins,” as taught by our esteemed faculty member, Dr. V.S. Kumar.
PROTEINS
Fibrous:
Elongated
Needle-like
Rod-like
Minimum solubility in H₂O
Structural
Example: Collagen, Elastin, Keratin
Globular:
Oval
Spherical in shape
Soluble in H₂O
Dynamic function
Example: Globulin, Albumin
Conjugated proteins:
Glycoproteins- Pro + Carb – TSH, FSH, LH
Metalloproteins- Pro + metal ion – Tyrosinase
– Carbonic Anhydrate
Neucleoproteins- Pro + N.Acid – Histones
Primary structure:
(Will never undergo dentuvation)
Relationship betwenn AA held together
Bond: Peptide bonds (Covalent bond)
Tech: Edman’s degradation
Sanger tech
→ Sanger Reagent – 1 – Fluoro- 2, -4- Dinitro Benzene
Mass spectrometry
2° structure:
Relationship between AA® C are about 3-4 AA Apart
Bond: H-bonds (non- Covalent)
(+) Electrostatic, Hydrophotic & Van Der Waals force
Tech: Circular dichromism
Optical rotatory dispersion chromatography
Example:
Alpha Helix
Beta-pleets
Loops
Bends
Turns
Super 2° structure:
Relationship between 2-2° structures
Combination of 2° structures
Example:
Helix-turn – Helix motif
Leuzin zipper- DNA binding motifs
Zinc zipper – DNA binding motifs
β-α-β motif
Tech: X-ray crystallography
NMR Spectroscopy
3° structure:
Relationship between AA lying at a distance
Bonds: Disulfide bonds
Hydrophobic, ionic interactions
4° structure:
Relationship between AA lying in different polypeptide chain
Bonds: H, Hydrophobic, Electrostatic, Van Der Waals force
Tech: Protein-Protein docking method
