Tertiary Structure of Protein - Medicinal Chemistry 1.7

Protein tertiary structure is the three-dimensional shape of a single polypeptide chain that could contain one or more secondary structures, such as alpha-helix, beta-sheet and beta-turn.
The main driving force of a polypeptide chain folding into its tertiary structure is the hydrophobic interactions, which lead to the formation of a hydrophobic core and a hydrophilic surface for most proteins.
There are several factors that stabilize the protein tertiary structure: 1. the van der Waals forces among the non-polar amino acid side chains and the protein backbone; 2. the hydrogen bonding between the polar side chains that carry a H-bond donor and a H-bond acceptor; 3. the electrostatic interactions between charged amino acid side chains; 4. the formation of disulfide bridge or disulfide bond between oxidized cysteine residues.
0:00 Tertiary structure
1:59 Hydrophobic interactions
3:16 van der Waals interactions
4:09 Hydrogen bonding
4:37 Electrostatic interactions
5:01 Disulfide bond/bridge
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I am a computational chemist in the pharmaceutical industry. I created the Mole Man Chem channel to explain some basic medicinal and biochemistry concepts because I believe the best way to relearn a concept is through teaching.
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[@isythnic7574]

Great stuff man, currently doing my VCE Yr12 biology and I've watched many videos however this one explains everything very clearly others try to keep it simple or too complicated.