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Science of Living System: Arindam Mondal
Science of Living System: Arindam Mondal
Living System
BS20001
Arindam Mondal
School of Bio Science
Email:
arindam.mondal@iitkgp.ac.in
Tel: 03222-260516
Protein Structure, Function, Kinetics
and Energetics
Books Followed:
CCTGAGCCAACTATTGATGAA
RNA: Transmission Medium
Polymer of nucleotides
CCUGAGCCAACUAUUGAUGAA
PEPTIDE
Amino acids: Building blocks of Proteins
Cα Cα
TRANS
H H
Cα Cα
CIS
Cα Cα
Torsion angles: Φ (phi) and Ψ (psi)
Peptide Plane
O R H
? C ? C ? N ?
C N ? C ? C
R H O R
Visualizing a few torsion angles
Front Back
1 4 4 (behind 1)
1
2 3
2
3 (behind 2)
Visualizing a few torsion angles
4 1 Front Back 4
1
0°
2 3
2
3
1 1 Front Back
4 4 Atom 4 is above
+45° the plane of the
2 3
board
Visualizing a few torsion angles
1 1 Front Back
4 4 Atom 4 is below
-45° the plane of the
2 3
board
1 1 Front Back
Atom 4 is below
-135° the plane of the
2 3
board
4
4
Ramachandran Plot
G. N. Ramachandran
Φ Ψ
Ψ (psi)
Φ (phi)
ɸ,Ψ= 0,0 is forbidden in any protein
Ramachandran Plot
α-Helix
β-Strand
Ψ (psi)
Φ (phi)
Glycine residues can adopt many
different conformations
Properties of Glycine
1
The protein folding problem
- Consider a small protein with 100 residues.
- Clearly, it would take too long for even a small protein to fold
properly by randomly trying out all possible conformations.
The main driving force for folding water soluble globular protein
molecules is to pack hydrophobic side chains into the interior of
the molecule, thus creating a HYDROPHOBIC CORE and a
HYDROPHILLIC SURFACE.
Thermodynamic hypothesis of
Protein Folding: The interactions
between the atoms in a protein control
the folding of the protein molecule into
a well-defined three-dimensional
structure.
Primary
Secondary
Tertiary
Quaternary
Secondary Protein Structure
Characterized by main chain NH and CO groups participating in H-bonds
Beta Sheet
Alpha helix
Alpha Helix
Less Preferred:
Pro, Gly, Tyr, Ser
Alpha Helix: Right-handed or Left-handed?
C
Hydrophobic
Hydrophilic
Charged
• Structure Function
• Structure Mechanism
• Structure Origins/Evolution
• Structure-based Drug Design
• Solving the Protein Folding Problem
H: α-helix
E: β-strand
QHTAWCLTSEQHTAAVIWDCETPGKQNGAYQEDCA
HHHHHHCCEEEEEEEEEEECCHHHHHHHCCCCCCC C: unstructured
Importance of Protein Structure
Hemoglobin A: Val-His-Leu-Thr-Pro-Glu-Glu-Lys-
Hemoglobin S: Val-His-Leu-Thr-Pro-Val-Glu-Lys-