Protein Structures

ABIA STATE UNIVERSITY, UTURU
P.M.B. 2000
FACULTY OF BASIC MEDICAL SCIENCES
DEPARTMENT OF MEDICAL LABORATORY SCIENCE
ASSIGNMENT ON
VARIOUS LEVELS OF ORGANIZATION OF PROTEIN
MOLECULES/STRUCTURES
PRESENTED BY
NAME: CHIDOZIEODU PEACE CHIKEZIRIM.
MATRIC NUMBER: 2018/116242/REGULAR
LEVEL: 200L
COURSE TITLE: CHEMISTRY AND METABOLISM OF
PROTEIN
COURSE CODE: BCM 242
LECTURER: MR KELECHI AKATAOBI UZOMA
DATE: 31st MARCH, 2021
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PROTEIN MOLECULES/STRUCTURES:
Protein structure is defined as a polymer of amino acids joined by peptide bonds.
There are four levels of protein structure namely
Primary structure
Secondary structure
Tertiary structure
Quaternary structure
1. PRIMARY STRUCTURE:
Primary structure of protein molecules is the specific, genetically determined order
of arrangements of amino acid residue in its polypeptide structure. It is popularly
referred to as the chemical structure of protein because it is stabilized by covalent
bond, which includes the peptide bonds of the polypeptide skeleton, disulphide and
isopeptide bridges involving the side chains where applicable.
The primary structure of protein is determined in series of experimental operations
called amino acid sequencing of proteins. It is a linear unbranched structure when
solely in the primary level of organization, the protein does not possess it's
characteristic biological activity. To get it to be fit into the cell and cellular structures,
and to get it carry out its biological function, the primary structures must be
appropriately folded into compact structure.
Image depicting Primary structure of Protein molecule.
2
2. SECONDARY STRUCTURE:
The secondary level of protein molecular organization is consequent upon the
development of intrachain hydrogen bonds between orderly arranged peptide bond in
the polypeptide structure. The sine qua non for maximum interaction of electronic
clouds at the peptide bond is the coplanar disposition of atoms at the bond.
The coplanar arrangement of atoms causes the keto oxygen of the bond to be
partially negatively charged while hydrogen atom of the NH group is partially
positively charged. This permits peptide bond units situated at a distance to develop
hydrogen bonds with each other.
Image depicting Secondary structure of Protein molecule.
The secondary structure is made up of two different types namely,

α-spiral structure
β-pleated sheat structure
α-spiral structure: This is a structure of definite geometry and dimensions. It is
formed consequent upon spiral winding of the peptide bond planes, around a
hypothetical cylinder. Stabilization of the α-spiral belongs to the intrachain hydrogen
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bonds which link distant peptide bond units in the structure.
These intrachain hydrogen bonds which occur parallel to the axis of the spiral, are
formed between every with peptide bond position of the spiral. As the intrachain
hydrogen bonds occur parallel to the axis of the spiral, amino acid radicals protrude
outward and at angle to the spiral axis.
An important feature of the polypeptide region with α-spiral structure is that it is
extremely densely packed this means that there are no empty spaces within the
hypothetical cylinder. The structure is characterized by what is called pitch, or a turn
of spiral, by this we mean the length of the segment through which the structure
geometrically repeats itself.
α-spiral structure is also called α-helix structure and it occurs within the limit of a
single polypeptide chain. A protein molecule at α-spiral level of structural
organization does not possess biological activity
β-pleated sheat structure: In this arrangement, the polypeptide chains are stretched
out beside one another and then bonded by intermolecular H-bonds.
The β-pleated sheat structure differs from the α-spiral in several respects. Two
structurally autonomous polypeptide chains can be involved in the formation of the β-
pleated sheat structure. The amino acid radicals in the β-pleated sheat structure are
situated above and below the general plane of the structure with the α-carbon atoms
located at the meeting line corrugations of the peptide bond planes; the hydrogen
bonds between peptide units runs perpendicular to the main axis of the polypeptide
structure.The β-pleated sheat structure is made up of two types namely;
-Parallel β-pleated sheat structure
-Antiparallel β-pleated sheat structure
Parallel β-pleated sheat structure: They are formed when polypeptide chains of the
interacting region of the molecule run in thesame direction. α-keratin, component of
the nitrogen fixation system of bacteria, and protein flavodoxin contains parallel β-
pleated sheat structure.
4
Antiparallel β-pleated sheat structure: They are formed when extended segment of
a polypeptide chain or polypeptide chains are aligned in the opposite direction. It may
involve two polypeptide chains or a single chain which changes direction and folds
back upon itself. Such changes in chain direction can be stabilized and caused by
proline , glycine charged residue and disulphide bridges
3. TERTIARY STRUCTURE:
This is a function of primary and secondary structurs. The peptide bonds and the
hydrogen bonds between the peptide units together with the interaction involving
adjacent and distant radical group makes up the totality of the spatial forces folding
the tertiary structure. Hydrogen bonds, electrostatic forces disulphide linkages and
Vander Waal's forces stabilizes the structure.
There are bases to postulates that the formation of the tertiary structure of the protein
molecule in vivo is an automatic process. The driving forces that governs the process
is the interaction of the structural elements of the polypeptide chain with molecules of
the dispersion medium, water the same forces are responsible for the spontaneous
organization of lipid molecule into bi-layers. During this process, hydrophobic amino
acid radicals are orientated into the interior of the molecule, whereas the hydrophilic
radicals are orientated into the exterior towards the water phase. This process is called
hydrophobic effect.
Tertiary structure of protein molecule occurs within the limit of a single polypeptide
chain and it possess biological activity.
5
Image depicting tertiary structure of Protein molecule
4. QUATENARY STRUCTURE: The spatial arrangement of various tertiary

structures gives rise to quaternary structure.
The formation of quant nary structure is a spontaneous process. The protomers of
multemeric molecules have complementary surfaces with which they specifically
interact with each other. The organization of multemeric protein molecules can
involve metallic ions and sometimes, low molecular weight organic compounds.
Structural integrity at quant nary level is maintained by weak physio-chemical forces,
namely:
Hydrogen bond
Hydrophobic effect
Vander Waal's forces
Electrostatic interaction
Two or more polypeptide chains may bind together to form a quaternary structure.
The quaternary structure of hemoglobin for instance, consist of four polypeptide
chains, two α, and two β subunits arranged in space in a defined manner. The
secondary, tertiary and quaternary structures of protein molecule are usually referred
to as the non-covalent molecular structures of protein.

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ABIA STATE UNIVERSITY, UTURU

FACULTY OF BASIC MEDICAL SCIENCES

DEPARTMENT OF MEDICAL LABORATORY SCIENCE

VARIOUS LEVELS OF ORGANIZATION OF PROTEIN

NAME: CHIDOZIEODU PEACE CHIKEZIRIM.

MATRIC NUMBER: 2018/116242/REGULAR

COURSE TITLE: CHEMISTRY AND METABOLISM OF

COURSE CODE: BCM 242

LECTURER: MR KELECHI AKATAOBI UZOMA

DATE: 31st MARCH, 2021

Image depicting Primary structure of Protein molecule.

Image depicting Secondary structure of Protein molecule.

The secondary structure is made up of two different types namely,

4. QUATENARY STRUCTURE: The spatial arrangement of various tertiary

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