LIFE 101

INTRODUCTION TO
BIOLOGY
Topic: Protein folding and some examples
Structure dictates function
Primary sequence structure
Protein folding: Levinthal’s paradox
100 amino acid polypeptide – 99 peptide bonds and
198 different φ and ψ angles

Assuming 10 different conformations for each amino

acid – 10100 different conformations

If each conformation is sampled – 1077 years

(assuming 10-13 second per conformation)

Protein folding – not a random, trial and error process

Protein folding

 https://doi.org/10.1002/anie.201713416
Stepwise protein folding
Assisted protein folding
[chaperones]
Assisted protein folding
[chaperones]
 Protein
unfolding
and refolding
Protein unfolding and denaturation
Protein misfolding and aggregation
Protein misfolding and diseases
Protein misfolding and diseases
Inhibitors of protein synthesis
[antibiotics]

https://courses.lumenlearning.com/microbiology/chapter/mechanisms-of-antibacterial-drugs/
Inhibitors of protein synthesis
[antibiotics]

https://courses.lumenlearning.com/microbiology/chapter/mechanisms-of-antibacterial-drugs/
Peptide hormones: Leptin
Produced by cells in small intestine
Energy Homeostasis; inhibits hunger
 Peptide hormones: Insulin
Produced by beta-cells of
pancreas. Regulates
carbohydrate & protein
metabolism. Absorption
of glucose from blood.
 Peptide hormones: Oxytocin
Secreted by the
posterior lobe
of the pituitary
gland.

Also known as
the "cuddle
hormone" or
the "love
hormone.
Prog Neurobiol. 2009 Jun; 88(2): 127–151.
Peptide hormones: Angiotensin II
Causes vasoconstriction (i.e. narrowing of blood
vessels) leading to hypertension.
 Green Fluorescent Protein (GFP)
Composed of 238 amino acids and exhibits bright
green fluorescence upon exposure to blue or UV light.
Originally identified and isolated from Jellyfish
Aequorea victoria.
Green Fluorescent Protein (GFP)
 Summary
- Protein folding (spontaneous folding and
chaperone-assisted folding)

- Examples of different proteins (hormones, Green

fluorescent protein)