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 Ramachandran plot – to visualize the
backbone of aminoacid residues
 Used for structural validation and to
calculate the possible phi and psi angles that
accounts for the aminoacid residues
 Done by several software namely
WHATIF RAMACHANDRAN PLOT
 Work of Ramachandran
 Initially proposed a modelled structure on
collagen as a two bonded system based on
the formation of two inter hydrogen bonds
between their structures
Basics of map
 Parameter – torsion angle
 System used – protein chain consisting
of aminoacid side chains
 Ramachandran angles
– phi and psi
A B C D
B C
A D
Peptide Bond & Phi-Psi Angles
Phi is the angle around the N-Ca bond
Psi is the angle around the Ca-C’ bond
Principle within the
formation
 Using the analysis of crystal structure
data two limiting condition was
approached
-normal limits
-outer limits
 Using phi and psi angles conformation
of linked peptide units are calculated
 This results in 3 conditions
The red, brown, and yellow regions represent the
favored, allowed, and "generously allowed" regions
Distribution over the map
 The distribution of phi and psi angles
for a total of 9,156 amino acid
residues from 4,413 protein chains,
based on crystallographic data
 2 areas where the density of points is
high
(1) Around phi= -60 and psi= -60
corresponds to the a-helix
(2) Around phi= -90 and psi= -120
corresponds to the b-structure
Aminoacid preferences
 Usually glycine and proline are not
peffered in ramachandran plot.
 The aminoacids with larger side chains
will show less number of allowed region
within the ramachandran plot.
 Proline gives a very less number of phi
and psi values since the possess five
carbon ring.
Thank you

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Ramachandran plot

  • 1.
  • 2.  Ramachandran plot – to visualize the backbone of aminoacid residues  Used for structural validation and to calculate the possible phi and psi angles that accounts for the aminoacid residues  Done by several software namely WHATIF RAMACHANDRAN PLOT
  • 3.  Work of Ramachandran  Initially proposed a modelled structure on collagen as a two bonded system based on the formation of two inter hydrogen bonds between their structures
  • 4. Basics of map  Parameter – torsion angle  System used – protein chain consisting of aminoacid side chains  Ramachandran angles – phi and psi A B C D B C A D
  • 5. Peptide Bond & Phi-Psi Angles Phi is the angle around the N-Ca bond Psi is the angle around the Ca-C’ bond
  • 6. Principle within the formation  Using the analysis of crystal structure data two limiting condition was approached -normal limits -outer limits  Using phi and psi angles conformation of linked peptide units are calculated  This results in 3 conditions
  • 7. The red, brown, and yellow regions represent the favored, allowed, and "generously allowed" regions
  • 8. Distribution over the map  The distribution of phi and psi angles for a total of 9,156 amino acid residues from 4,413 protein chains, based on crystallographic data  2 areas where the density of points is high (1) Around phi= -60 and psi= -60 corresponds to the a-helix (2) Around phi= -90 and psi= -120 corresponds to the b-structure
  • 9. Aminoacid preferences  Usually glycine and proline are not peffered in ramachandran plot.  The aminoacids with larger side chains will show less number of allowed region within the ramachandran plot.  Proline gives a very less number of phi and psi values since the possess five carbon ring.