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Protein Folding

Proteins fold into complex 3D structures driven by non-covalent interactions like hydrogen bonding and hydrophobic interactions. Molecular chaperones assist in protein folding by binding to unfolding proteins and preventing incorrect folding and aggregation. Proper folding progresses from primary structure determined by gene sequence to secondary structures like alpha helices and beta sheets and then to tertiary and quaternary structures which are stabilized by various interactions and determine the protein's final shape and function.

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380 views13 pages

Protein Folding

Proteins fold into complex 3D structures driven by non-covalent interactions like hydrogen bonding and hydrophobic interactions. Molecular chaperones assist in protein folding by binding to unfolding proteins and preventing incorrect folding and aggregation. Proper folding progresses from primary structure determined by gene sequence to secondary structures like alpha helices and beta sheets and then to tertiary and quaternary structures which are stabilized by various interactions and determine the protein's final shape and function.

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isaiah tariq
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Protein Folding

• Proteins fold into one or more specific spatial conformations


driven by a number of non-covalent interactions such as
hydrogen bonding, ionic interactions, Van der Waals forces,
and hydrophobic packing.
• A polypeptide folds into its characteristic 3D structure from a
random coil.
• After translation the linear chain begins to fold into its three-
dimensional structure.
• Several neurodegenerative and other diseases
are believed to result from the accumulation
of amyloid fibrils formed by misfolded
proteins.
• Many allergies are caused by incorrect folding
of some proteins, because the immune system
does not produce antibodies for certain
protein structures.
Protein folding depends on;
• Solvent (water or lipid bilayer)
• Temperature
• pH
• Concentration of salt
• the possible presence of cofactors
• Molecular cheperons
Role of Cheperones
• Molecular chaperones are a class of proteins that aid in the
correct folding of other proteins.
• Chaperones exist in all cellular compartments and interact
with the polypeptide chain in order to allow the native 3D
conformation of the protein to form.
• Chaperones prevent aggregation and incorrect folding by
binding to and stabilizing partially or totally unfolded
polypeptides until the polypeptide chain is fully synthesized.
• Ensure the stability of unfolded chains.
• Each of the families of molecular chaperones
have their own functions e.g. the “heat shock
proteins” (Hsps), particularly the Hsp70 and
Hsp60 families.
Protein Structure
• Protein structure is the 3D arrangement of
atoms in an amino acid-chain.
• Under condensation reactions, amino acids lose
one water molecule per reaction in order to
attach to one another with a peptide bond.
• Protein structures range in size from tens to
several thousand amino acids.
• A protein usually undergoes reversible structural
changes in performing its biological function.
Process of protein folding
Following are some levels of Protein structure.
• Primary structure.
• Secondary structure.
• Tertiary structure.
• Quaternary structure.
Primary structure
• The primary structure is held together by peptide bonds that
are made during the process of protein biosynthesis.
• Reaction take place by peptide linkage between Amino group
(-NH2) of one amino acid to the Carboxyl group (-C=0) to the
next amino acid and water is produced.
• The primary structure of a protein is determined by the gene
corresponding to the protein.
• The sequence of amino acid residues can be read directly
from the sequence of the gene using the genetic code.
Secondary structure
• Formation of a secondary structure is the first step in the
folding process.
• The two most common secondary structural elements are;
alpha helices and beta sheets.
Alpha helices.
The amino acids in an α-helix are arranged in a right-handed
helical structure where each amino acid residue corresponds to
a 100° turn in the helix. In a right hand-helix conformation in
every backbone N−H group hydrogen bonds to the backbone
C=O group.
Beta sheets; secondary fold
• The β pleated sheet is a structure that forms with the
backbone bending over itself to form the hydrogen
bonds.
• The hydrogen bonds are between the amide hydrogen
and carbonyl oxygen.
• There exists anti-parallel β pleated sheets and parallel
β pleated sheets, hydrogen bonds are strongly stable
in the anti-parallel β sheet as it hydrogen bonds with
the ideal 180 degree angle compared to the slanted
hydrogen bonds formed by parallel sheets.
Tertiary structure
• The α-helixes and β-pleated-sheets are folded into a compact
globular structure.
• The folding is driven by hydrophobic interactions.
• It is generally stabilized by outside polar hydrophilic hydrogen
and ionic bond interactions, and internal
hydrophobic interactions.
• Tertiary folding begins while the protein
is being molded into its
primary polypeptide sequence.
• It is known to be guided
by chaperones.
Quaternary structure
• Quaternary structure is the arrangement of more than one
protein molecule in a multi-subunit complex.
• These subunits may be the same, as in a homodimer, or
different, as in a heterodimer.
• The final shape of the protein complex is once again stabilized
by various interactions, including hydrogen-bonding, disulfide-
bridges and salt bridges.
• Forexample hemoglobin.
• In hemoglobin, one protein
binds to oxygen while another
binds carbon dioxide.

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