B1.2 Proteins
First Exams 2025 B1.2 Proteins
Theme: Form and Function
Level of Organisation: Molecules
Power of Science
SL and HL Combined Content
Focus on understanding the power of science relating to proteins.
IB Guiding Questions
What is the relationship between amino acid sequence and the diversity in form and function of proteins?
How are protein molecules affected by their chemical and physical environments?
Content Overview
B1.2 Proteins
B1.2.1: Generalized structure of an amino acid
B1.2.2: Condensation reactions forming dipeptides and longer chains of amino acids
B1.2.3: Dietary requirements for amino acids
B1.2.4: Infinite variety of possible peptide chains
B1.2.5: Effect of pH and temperature on protein structure
Key Terms
Amino Acid
Amine Group
Carboxylic Acid Group
Side Chain (R Group)
Condensation Reaction
Dipeptide
Peptide Bond
Polypeptide
Essential Amino Acids
Non-Essential Amino Acids
Genetic Code
Denaturation
Generalized Structure of Amino Acids
Components include:
Amine Group (-NH2)
Hydrogen atom
Central alpha carbon
Carboxyl group (-COOH)
Side chain (R Group)
Twenty Amino Acids
All organisms utilize the same twenty amino acids for protein synthesis.
Each amino acid has unique R groups which determine their properties.
Formation of Dipeptides
Condensation reaction:
Amino Acid + Amino Acid → Dipeptide + Water
A peptide bond forms between the carbon of the carboxylic acid and the amine group of another amino acid.
Amino Acid Models
To understand structures, diagrams and molecular models can be used (e.g., Molview).
Polypeptides
A long chain of amino acids formed through multiple condensation reactions during translation.
Dietary Requirements
Essential vs. Non-Essential Amino Acids
Essential amino acids must be obtained from food, while non-essential amino acids can be synthesized by the body.
Vegan diets need to ensure the intake of all essential amino acids through diverse plant sources.
Proteins and the Genetic Code
DNA codes for polypeptides; sequences can vary significantly leading to diverse proteins.
Protein Denaturation
Defined as a conformational change that results in loss of function, influenced by extreme pH and temperature changes.
Quaternary Structure
Exists in proteins with more than one polypeptide chain held together by various interactions (hydrogen, ionic, etc.).
Protein Examples
Non-Conjugated Proteins
Insulin: Hormonal regulation of glucose, composed of two polypeptide chains linked by disulfide bridges.
Collagen: Structural protein found in connective tissues, consisting of three polypeptide chains forming a triple helix.
Conjugated Proteins
Haemoglobin: Composed of multiple polypeptide chains and non-polypeptide groups (heme), it has a crucial role in oxygen transport.
Form and Function
Distinctions in globular and fibrous proteins influence their specific roles within living organisms (e.g., insulin vs. collagen).
Additional Notes
Students should recognize that the R-group variations affect protein structure and function, impacting interactions and protein folding.