Understanding Proteins:Building block of life

Prepared by: Hafiz Muhammad Yousaf baig (221610)

Hafiz Muhammad Usman (221637)
Zuhaa Ejaz Kazmi (221630)
Anas Ejaz
Syed Anees Asad (221617)
SUBMITTED TO
ENGR.BATOOL ZAHRA

Department of Biomedical Engineering , Air University Islamabad

Presentation Contents

 Introduction of protein
 Classification of protein
 Structures of protein
 Conclusion
 Introduction of Protein

Protein:
 Proteins are large, complex molecules composed of amino acids.
 Amino acids are the building blocks of proteins, characterized by an amino group,
a carboxyl group, and a unique side chain.
 Proteins have a diverse range of structures and functions, dictated by their
amino acid sequence.
 Classification of Proteins

The proteins are broadly classified into two

types:
• Fibrous protein
• Globular protein
Fibrous Protein
• elongated, insoluble molecules primarily responsible for providing structural support.
• They form elongated fibers or sheets within cells and tissues.

• collagen, keratin, fibroin, and elastin.

• These proteins contribute to the integrity and functionality of various tissues, including
tendons, skin, hair, and connective tissues.

• Essential for maintaining the structural integrity and mechanical properties of cells and
tissues in living organisms.
Globular Protein

• compact, water-soluble molecules with a spherical shape,

characterized by their folded structure.
• They exhibit a rounded or globular shape.
• globular proteins are soluble in water and polar solvents.
• These proteins play diverse roles in biological processes, including
enzymatic catalysis, molecular transport, cellular regulation, and
immune response.
• Hemoglobin, insulin, lysozyme, and catalase are examples of
globular proteins.
 Structure of Proteins

 Primary Structure
 Secondary Structure
 Tertiary Structure
 Quantatery Structure
 Primary Proteins
• Sequence of amino acids in a protein's
polypeptide chain.

• DNA-encoded sequence.

• Minor changes in primary structure can greatly

affect protein function

• They are Hydrophobic in nature due to the outer

layering of chain.
Secondary Structure
• Secondary structure refers to local folding patterns in a protein's
polypeptide chain.
• secondary structures are alpha helices and beta sheets.
• Alpha Helices: Formed by twisting the chain into a right-handed coil,
with hydrogen bonds between adjacent amino acids.
• Beta Sheets: Comprise extended strands running alongside each other, with
hydrogen bonds between adjacent strands.
• Secondary structure contributes to protein's overall three-dimensional
conformation, impacting function and stability.
• Hydrogen bonds between backbone atoms of amino acids stabilize secondary
structures.
Tertiary structure

 Tertiary structure reflects the functional conformation of

polypeptides, presenting a distinctive 3D shape with surface
functional groups for molecular interactions.
 Chaperones assist in positioning amino acids for bond formation
 4 main interactions are involved in tertiary structures:
• Hydrophobic interactions
• Disulfide bridges
• Ionic bonds
• Hydrogen bonds
Quaternary structure

 The quaternary structure of proteins involves the arrangement and

interaction of multiple folded polypeptide chains.
 The polypeptide chains may be identical or they may be very
different from each other.
 The main interactions in quaternary structures are noncovalent
interactions, hydrogen bonds, ionic interactions, disulfide bonds
and hydrophobic interactions
 Conclusion

• Proteins are versatile molecules with intricate structures and diverse functions.
• Understanding protein classification and structure is essential for elucidating their
roles in biological processes.
• Further research into protein structure-function relationships holds promise for
advancing fields such as medicine, biotechnology, and drug discovery.