Amino Acids Classification and Protein Primary Structure - Medicinal Chemistry 1.4

There are 20 common amino acids found in humans. Each amino acid has a carbonyl group, an amino group and a side chain attached to its alpha-carbon. Based on the types of side chains, amino acids can roughly be divided into different categories, such as polar or non-polar, charged or uncharged, etc.
Amino acids can be linked together via peptide bonds to form polypeptide chains. The primary structure of a protein is referring to the order or the sequence of the amino acid residues that make up the protein.
As the building blocks of proteins and polypeptides, amino acids play a vital role in drug design targeting proteins. Chemists come up with different strategies and compound analogs based on the amino acid residues present in the protein binding pocket.
Please feel free to leave your questions and suggestions in the comments and I will get back to you.
0:00 Overview
0:23 Amino acids
1:07 Primary structure
2:27 Charged amino acids
3:43 Polar amino acids
4:48 Cysteine
6:34 Proline and glycine
7:11 Hydrophobic amino acids
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[@molemanchem4385]

Understanding the properties of amino acid residues in the ligand binding pocket is very important to structure-based drug design (SBDD). SBDD is using the knowledge of the three-dimension space of the binding pocket to optimize the interaction between the drug and the biomolecule target.

[@Lily144atpase]

Thank u

[@whengale]

Thank you for posting this!
Something I'm a little confused about: you stated around 1:04 that a peptide bond is formed via "a dehydrogenation or condensation reaction". Isn't dehydrogenation the removal of JUST hydrogen? So, it wouldn't actually be a dehydrogenation reaction in the case of a peptide bond forming?

[@aristarchussmeda]

Thx