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Understanding Proteins and Biomolecules
Sep 5, 2024
Lecture Notes: Proteins and Related Biomolecules
Overview of Proteins
Found in:
Meat and legumes
Composition:
Carbon, oxygen, hydrogen, nitrogen, and some sulfur
Role:
Construction materials for the body; body's workers
Properties:
Hydrophilic, dissolve in water
Amino Acids and Protein Structure
Building Blocks:
20 amino acids
8 essential amino acids (must be obtained from diet)
Polypeptides:
Chains of up to 50 amino acids
Longer chains are proteins
Structure Levels:
Primary Structure:
Sequence of amino acids
Secondary Structure:
Hydrogen bonds form shapes like helix or pleated sheets
Tertiary Structure:
3D folds due to hydrogen and covalent bonds
Quaternary Structure:
Combination of multiple tertiary structures (e.g., hemoglobin)
Function:
Specific to protein's amino acid sequence
Types of Proteins
Fibrous Proteins:
Structural
Provide strength, e.g., collagen, keratin
Tendons, skin, hair, nails
Globular Proteins:
Functional
Compact, spherical
Include antibodies, hormones, enzymes
More delicate compared to fibrous proteins
Enzymes
Role:
Biological catalysts
Function:
Increase reaction rate, do not become part of products
Active Sites:
Bind reacting molecules, assist in breaking/making bonds
Specificity:
Shape determines function
Naming:
Often ends in "-ase" (e.g., hydrolysis, oxidases)
Inactive Forms:
Often produced in inactive forms (e.g., pepsinogen)
Nucleic Acids
Types:
DNA, RNA
Function:
Genetic material, blueprint for proteins
DNA Structure:
Double helix
Nucleotides:
Adenine, thymine, guanine, cytosine
Complementary base pairs: A-T, G-C
RNA:
Single-strand, involved in protein synthesis
Uracil replaces thymine
ATP (Adenosine Triphosphate)
Role:
Energy molecule of the body
Structure:
Adenosine with three phosphates
High-Energy Bonds:
Release energy when broken
ATP to ADP:
Energy release through hydrolysis
Recharging:
Phosphates reattached using energy from food oxidation
Conclusion
Next topic: Cells
Break before continuing
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