SUBMITTED BY: ARHAM AHMAD
SAP ID: 057000
SUBJECT: BIOCHEMISTRY I
SUBMITTED TO: DR FATIMA TARIQ
TOPIC: STRUCTURE OF PROTEINS
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Introduction to Proteins
Proteins are essential biomolecules in all living organisms, playing roles in structure, transport,
signaling, enzymes, and immune defense. Composed of amino acids, proteins acquire complex
shapes that allow them to perform specific functions. The structure of a protein determines its
function, and understanding these structures can provide insight into how proteins work and how
they can be altered or targeted in fields like medicine and biotechnology.
1. Primary Structure of Proteins
The primary structure of a protein is the unique sequence of amino acids in a polypeptide chain.
Each amino acid is connected by a peptide bond formed between the amino group of one amino
acid and the carboxyl group of the next. This sequence is encoded by the gene for that protein
and is crucial for determining the higher levels of structure. Even a single amino acid change can
sometimes drastically affect a protein's function (e.g., in sickle cell anemia).
2. Secondary Structure of Proteins
Secondary structure refers to local folding patterns within the polypeptide chain, primarily
stabilized by hydrogen bonds. Two common types of secondary structures are alpha helices and
beta sheets.
Alpha Helix
• An alpha helix is a coiled structure that resembles a spring or a helix.
• Stabilized by hydrogen bonds between the carbonyl oxygen of one amino acid and the
amide hydrogen four residues down the chain.
• This pattern creates a right-handed spiral structure, with side chains pointing outward.
• Alpha helices are common in structural proteins, such as keratin (found in hair and nails),
and in many enzymes.
Beta Sheet
• In beta sheets, the polypeptide chain folds back on itself, forming a sheet-like structure.
• Hydrogen bonds occur between backbone atoms of different strands, which can be
aligned in parallel (same direction) or anti-parallel (opposite directions).
• Beta sheets are typically flat or twisted and contribute to the stability and strength of
structural proteins, such as silk fibroin.
Beta Bend
• A beta bend (or turn) is a sharp turn in the polypeptide chain that often links different
secondary structures, like alpha helices or beta sheets.
• It allows the polypeptide to reverse direction and is stabilized by hydrogen bonds.
• Beta bends are typically found on the protein's surface, aiding in compact folding and
enabling interactions with other molecules.
3. Tertiary Structure of Proteins
The tertiary structure is the overall 3D shape of a single polypeptide chain, formed when
secondary structures fold into a complex, functional form. This structure is stabilized by various
interactions:
• Hydrophobic interactions between nonpolar side chains.
• Hydrogen bonds between polar side chains.
• Ionic bonds between charged side chains.
• Disulfide bridges (covalent bonds) between cysteine residues.
The tertiary structure is essential for the function of enzymes and other proteins, as it forms the
active site where specific substrates bind.
4. Supersecondary Structure of Proteins
Supersecondary structures are combinations of alpha helices and beta sheets that form
recognizable patterns. These include:
• Beta-alpha-beta motifs: A beta sheet connected to an alpha helix by a short loop.
• Helix-turn-helix motifs: Two alpha helices connected by a turn, commonly found in
DNA-binding proteins.
• Greek key motif: Four beta strands folded to resemble a Greek key pattern.
These patterns contribute to the stability and function of the protein and are often involved in the
formation of specific binding sites or structural scaffolds.
