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Structure of Proteins
Fundamentals of Protein
Structure
Introduction
• Proteins are major components of all
cellular systems
• Proteins consist of one or more
linear polymers called polypeptides
• Proteins are linear and never
branched
• Different AA’s are linked together
via PEPTIDE bonds
• The individual amino acids within a
protein are known as RESIDUES
• The smallest known Peptide is just
nine residues long - oxytocin
• The largest is over 25,000 residues -
the structural protein titin
Classification of proteins
A. Functional Basis
Nothing can compare with the versatility of proteins. Their functionality and usage
in organisms is unrivalled.
•Ψ and φ angles will cause the hydrogen and oxygen and other
residue to collide
•Many chain rotations are restricted to Ψ and φ.
•This restricts the number of conformations in proteins
• Many angles of rotation are possible only a few are energetically
favorable
• By convention Ψ and φ are 180° (or –180°) when the first and
fourth atoms are farthest apart and the peptide is fully extended.
• In a protein, some of the conformations shown here (e.g., 0°)
are prohibited by steric overlap of atoms.
Ramachandran plots
•Ramachandran plot shows the distribution of f and y dihedral angles that
are found in a protein
•Some Ψ and φ combinations are very unfavorable because of steric crowding of
backbone atoms with other atoms in the backbone or side-chains.
•Some Ψ and φ combinations are more favorable because of chance to form
favorable H-bonding interactions along the backbone (Blue-shaded areas).
•shows the common secondary structure elements reveals regions with unusual
backbone structure
3 Major Types
• α-Helix
• β-Conformation or Sheets
• β-Turns
The a-helix • In the a-helix, the carbonyl oxygen of
residue “i” forms a hydrogen bond with
the amide of residue “i+4”.
• Small hydrophobic residues such as Ala and Leu are strong helix formers
• Pro acts as a helix breaker because the rotation around the N-Ca bond is
impossible
• Gly acts as a helix breaker because the tiny R group supports other conformations
Domain
A domain, is a part of a polypeptide chain that
is independently stable or could undergo
movements as a single entity with respect to the
entire protein.
Polypeptides with more than a few hundred
amino acid residues often fold into two or more
domains, sometimes with different functions
Quaternary structure = Higher-order assembly of proteins
• Quaternary structure is formed by spontaneous assembly of individual
polypeptides into a larger functional cluster
• Oligomeric Subunits (protomers) are arranged in Symmetric Patterns
* protomer is the structural unit of an oligomeric protein.
• The interaction between multiple polypeptides or prosthetic groups
• A prosthetic group is an inorganic compound involved in a protein (e.g.
the heme group in haemoglobin)
Examples of other quaternary structures
Tetramer Hexamer Filament