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What are the 6 Major Chemical Bonds or Interactions In Proteins?

6 Major chemical bonds in Proteins
In this post let me  give you a quick summary of major bonds in Proteins.
Proteins are biomolecules  made up of amino acids joined by peptide bond.
Different types of bonds interactions in protein structure

Bonds in protein:
1. Peptide bond
How is peptide bond formed in protein
  • Peptide bond is formed when a water  molecule is eliminated during a reaction between 
  • –NH2 (amino group) of one amino acid and –COOH (carboxyl group) of another.
Peptide bond or amide bond Characteristics

watch this video on peptide bond for more clarity of concept
  • Covalent bond that joins 2 amino acids
  • Dehydration synthesis: release of H2O
  • Partial double bond character: as shorter than a single bond
  • Rigid and planar: rotation around the bond is restricted
  • Trans configuration: less steric hindrances of adjacent amino acid side chains
  • Uncharged : only side chains and N and C terminals are charged.

2. Disulfide bonds: covalent bond formed between Sulphur containing amino acid
di sulphide bond formation in protein
  • It forms when the -SH groups of two cysteine residues are covalently linked as a dithiol by oxidation
  • It may be formed between different chains of amino acids or between different parts of the chain.
  • It provide some rigidity to the protein molecule.

3. Hydrophobic Bond 
Hydrophobic bond in protein formation
  • It is formed between two non polar groups or hydrophobic amino acids.
  • Hydrophobic bonding forms an interior, hydrophobic protein core, where most hydrophobic side chains can closely associate and are shielded from interactions with solvent water.
  • Most important driving force in protein folding

4. Hydrogen Bond
how is Hydrogen bond formed in protein
  • A hydrogen bond is the electromagnetic attractive interaction between polar molecules, in which hydrogen is bound to a highly electronegative atom, such as nitrogen, oxygen or fluorine. It is a weak bond.
  • Amino acids with side chain containing –OH, -NH2 etc participate in H-bonding
5. Ionic Bond 
How is ionic bond formed in protein
  • Ionic bond forms  due to attractive force between oppositely charged ionised groups. 
  • Refer the above figure where aspartic acid is negatively charged and lysine is positively charged
  • The Van der Waals force is a transient, weak electrical attraction of one atom for another. 
  • It is the sum total of all non covalent associations between electrically neutral molecules.
Watch this video on bonds in proteins for better understanding. Thank you
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