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12 views3 pages

Bio Summary

Uploaded by

ryan20001314
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© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Here’s a summary of the “Biological Molecules” presentation divided into sections:

1. Introduction to Biological Molecules

• Key molecules necessary for life: Carbohydrates, Proteins, Lipids, Nucleic Acids,
and Water.
• Carbohydrates, proteins, lipids, and nucleic acids are organic compounds
containing carbon (C) and hydrogen (H).

2. Covalent Bonds in Polymers

• Definition and types of covalent bonds: polar and nonpolar covalent bonds.
• Formation of covalent bonds through condensation reactions (creating
polymers/macromolecules and releasing water).
• Breaking covalent bonds through hydrolysis (adding water to break polymers).
• Types of covalent bonds relevant to biological molecules.

3. Carbohydrates

• Composed of carbon, hydrogen, and oxygen atoms in a specific ratio


(Cn(H2O)n).
• Types of carbohydrates: monosaccharides (e.g., glucose), disaccharides, and
polysaccharides.
• Structural forms of glucose (alpha and beta).
• Reducing and non-reducing sugars: Differences, detection using Benedict’s test.
• Glycosidic bonds and their role in forming disaccharides and polysaccharides.
• Polysaccharide structures and functions: Starch (plants), Glycogen (animals),
and Cellulose (structural component).

4. Lipids

• Contain carbon, hydrogen, and oxygen, but with less oxygen compared to
carbohydrates.
• Types of lipids: Triglycerides, Phospholipids, Steroids, and Waxes.
• Functions of triglycerides: energy storage, insulation, buoyancy, and protection.
• Phospholipids and their role in forming cell membranes (hydrophilic and
hydrophobic properties).

5. Proteins

• Made of amino acid monomers forming polypeptides.


• Formation of peptide bonds through condensation reactions.
• Protein structures:
• Primary Structure: Amino acid sequence.
• Secondary Structure: Hydrogen bonding forming alpha-helix or beta-pleated
sheets.
• Tertiary Structure: Further folding due to interactions among R-groups
(hydrophobic, disulfide, ionic bonds).
• Quaternary Structure: Multiple polypeptide chains (e.g., haemoglobin and
collagen).
• Comparison of globular (e.g., haemoglobin) and fibrous (e.g., collagen) proteins,
including their structures and functions.

6. Water

Polar molecule with a dipole nature.


Properties include being an excellent solvent, having high specific heat capacity, and high latent
heat of vaporization.

Structural Roles:
• Carbohydrates such as cellulose form strong fibers used in plant cell walls for
rigidity and support.
• Proteins like collagen provide strength and flexibility to connective tissues such
as tendons, cartilage, and skin.

Energy Storage and Metabolism:


• Lipids, particularly triglycerides, are energy-dense storage molecules, providing
long-term energy reserves in adipose tissue.
• Glycogen in animals serves as a readily available energy reserve in muscle and
liver cells.

Enzymatic Functions:
• Proteins play critical roles as enzymes, catalyzing biochemical reactions within
cells and across systems.
• Enzymes lower activation energy for reactions, speeding up essential metabolic
processes.

Cell Communication and Regulation:


• Proteins serve as hormones, cell membrane receptors, and signal transducers,
facilitating communication between cells and tissues.
• Lipids such as phospholipids form the basis of cellular membranes, maintaining
cell compartmentalization and controlling the movement of molecules.

Transport and Immune Defense:


• Hemoglobin (a globular protein) transports oxygen throughout the bloodstream in
animals.
• Immunoproteins, such as antibodies, are key to identifying and neutralizing
pathogens.

Water’s Role in Biological Systems:


• Serves as a universal solvent, facilitating biochemical reactions and nutrient
transport.
• High specific heat and vaporization properties help regulate temperature and
protect organisms from rapid temperature changes.

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