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Short range interactions and electrostatic forces
in Protein
BY : HEENA
BSC BIOTECHNOLOGY IIIRD YEAR
ROLL NO : 6604
What is Short Range Interactions?
 Interaction that occur between atoms or residues that are in
close proximity
 play role in :
Protein folding , protein stability.
 E.g.. :
1. Hydrogen bonds
2. Van der Waals forces
3. Hydrophobic interactions
4. Ionic interactions (salt bridge)
5. Disulphide bonds
Hydrogen bond
 Occur between a hydrogen atom bonded to an electronegative
atom
( nitrogen or oxygen)
 Weak (than covalent bonds).
 Creates relatively strong dipole dipole interaction between the H-
atom and electronegative atom .
 Plays role in :-
1. Protein folding
2. Stabilize secondary structure of proteins
by forming Hydrogen bonds between backbone atom of A.A
Hydrophobic effect
 Occurs between non polar or hydrophobic regions of
A. A
 In aq. Environment,
Hydrophobic amino acids tend to cluster together
to
minimize their exposure to water .
 Contribute to protein folding
 Helps in formation of protein cores.
Ionic Interactions
 Also called salt bridge
 occurs between –ve and +ve charged amino acid
residues.
 Contribute to stability of protein structure
 Role in protein – protein interaction.
Disulphide bonds
 Between 2 cysteine residues in protein
 Occur within a relatively small region of protein
 Provide structural stability
 Influence protein folding
Van der waal forces
 Also called London dispersion forces.
 Helps to hold things together.
 Commonly , Molecules have dipole .
 When 2 molecules come close their dipole attract each other and
hold the molecules together.
 In proteins,
1. These forces maintain the shape of protein.
2. Help in proper functioning of protein.
Electrostatic forces
 Also called : electrostatic interactions or columbic interactions
 attractive and repulsive forces between charged particles
 Arise from presence of A.A residues
 Amino acid:
1. +ve charged – Basic
2. -ve charges – Acidic
3. Uncharged – neutral
 2 main mechanism:-
1. Ion – ion interactions
2. Ion dipole interactions
 Ion – ioninteraction:
1. Occur when 2 charged residues come close
2. May be attractive or repulsive
3. Contribute in stability and protein folding
 Ion- dipole interaction:
1. Between charged residues and polar molecule (water)
2. Help in solubility and hydration of protein
Strength of electrostatic forces depends on :-
1. Distance between charged residues
2. magnitude of charge
3. Dielectric constant of surrounding material.
short range interaction for protein and factors influencing or affecting the proteins binding forces

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short range interaction for protein and factors influencing or affecting the proteins binding forces

  • 1. Short range interactions and electrostatic forces in Protein BY : HEENA BSC BIOTECHNOLOGY IIIRD YEAR ROLL NO : 6604
  • 2. What is Short Range Interactions?  Interaction that occur between atoms or residues that are in close proximity  play role in : Protein folding , protein stability.  E.g.. : 1. Hydrogen bonds 2. Van der Waals forces 3. Hydrophobic interactions 4. Ionic interactions (salt bridge) 5. Disulphide bonds
  • 3. Hydrogen bond  Occur between a hydrogen atom bonded to an electronegative atom ( nitrogen or oxygen)  Weak (than covalent bonds).  Creates relatively strong dipole dipole interaction between the H- atom and electronegative atom .  Plays role in :- 1. Protein folding 2. Stabilize secondary structure of proteins by forming Hydrogen bonds between backbone atom of A.A
  • 4. Hydrophobic effect  Occurs between non polar or hydrophobic regions of A. A  In aq. Environment, Hydrophobic amino acids tend to cluster together to minimize their exposure to water .  Contribute to protein folding  Helps in formation of protein cores.
  • 5. Ionic Interactions  Also called salt bridge  occurs between –ve and +ve charged amino acid residues.  Contribute to stability of protein structure  Role in protein – protein interaction.
  • 6. Disulphide bonds  Between 2 cysteine residues in protein  Occur within a relatively small region of protein  Provide structural stability  Influence protein folding
  • 7. Van der waal forces  Also called London dispersion forces.  Helps to hold things together.  Commonly , Molecules have dipole .  When 2 molecules come close their dipole attract each other and hold the molecules together.  In proteins, 1. These forces maintain the shape of protein. 2. Help in proper functioning of protein.
  • 8. Electrostatic forces  Also called : electrostatic interactions or columbic interactions  attractive and repulsive forces between charged particles  Arise from presence of A.A residues  Amino acid: 1. +ve charged – Basic 2. -ve charges – Acidic 3. Uncharged – neutral  2 main mechanism:- 1. Ion – ion interactions 2. Ion dipole interactions
  • 9.  Ion – ioninteraction: 1. Occur when 2 charged residues come close 2. May be attractive or repulsive 3. Contribute in stability and protein folding  Ion- dipole interaction: 1. Between charged residues and polar molecule (water) 2. Help in solubility and hydration of protein
  • 10. Strength of electrostatic forces depends on :- 1. Distance between charged residues 2. magnitude of charge 3. Dielectric constant of surrounding material.