We Solved the Protein Folding Problem… Now What?
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Top Comments (10)
I was genuinely curious to what Max was saying and you guys kept interrupting him and not letting him finish - it's painful to watch...
4:42 “this pixel, this pixel, this pickle”
Chuck is such a renaissance man. His questions are always so insightful yet accessible and he'll manage to make us laugh at the same time. Good stuff!
PhD in biochemistry and molecular biophysics here. I absolutely love this conversation to share with the general the general public to demystify this topic. I want to add another layer regarding the molecular basis of protein folding. The amino acids that Max Jaderberg mentioned are comprised of atoms like Carbon, Nitrogen, and Oxygen (with some two containing Sulfur). In an amino acid, the Nitrogen atom can exhibit a positive charge, while the Oxygen can exhibit a negative charge. Since opposite charges attract, an amino acid for example in the start of the string can interact with an amino acid farther down the string, thus "folding" the string. This is called electrostatic interactions of amino acids. When these proteins are being made in the cell, they are assembled one amino acid at a time by a molecular machine (called the ribosome) where you can think about it as a sort of a conveyer belt emerging from a sorting box. Because these amino acids are incorporated one at a time, the charges of the first amino acid would interact would the charges of the second amino acid attached immediately. Then as more amino acids are added and the string gets longer, the electrostatic landscape of the string changes and creates more intricate folding to optimally pair opposite charges. The protein fold that is the final product represents the most stable pairing of positive and negative charges. Therefore, when it comes to human disease that arise from amino acid mutations in the string, this disrupts how the protein would normally fold and results in a unstable protein that would then either not do the job its supposed to do or get thrown to the garbage can of the cell. Apologies for the lengthy explanation!
If AI could design custom medicines just for you, firstly would you trust it? Secondly, what kind of breakthrough would you hope it solves (i.e. cancer, aging, rare diseases, or something else)?
This is the kind of news that needs to go viral.
"To a jelly fish we all look the same" - Neil Tyson
Look at Chuck bringing the real questions!
Chuck is self deprecating, but has some of the best insights and questions of anyone out there.
When I was a kid, my dad was a chemist and he DID come home smelling like chemicals. My mom would make him undress in the garage after he came home and out his clothes directly in the closet. He worked on acetaminophen.
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Top Comments (10)
I was genuinely curious to what Max was saying and you guys kept interrupting him and not letting him finish - it's painful to watch...
4:42 “this pixel, this pixel, this pickle”
Chuck is such a renaissance man. His questions are always so insightful yet accessible and he'll manage to make us laugh at the same time. Good stuff!
PhD in biochemistry and molecular biophysics here. I absolutely love this conversation to share with the general the general public to demystify this topic. I want to add another layer regarding the molecular basis of protein folding. The amino acids that Max Jaderberg mentioned are comprised of atoms like Carbon, Nitrogen, and Oxygen (with some two containing Sulfur). In an amino acid, the Nitrogen atom can exhibit a positive charge, while the Oxygen can exhibit a negative charge. Since opposite charges attract, an amino acid for example in the start of the string can interact with an amino acid farther down the string, thus "folding" the string. This is called electrostatic interactions of amino acids. When these proteins are being made in the cell, they are assembled one amino acid at a time by a molecular machine (called the ribosome) where you can think about it as a sort of a conveyer belt emerging from a sorting box. Because these amino acids are incorporated one at a time, the charges of the first amino acid would interact would the charges of the second amino acid attached immediately. Then as more amino acids are added and the string gets longer, the electrostatic landscape of the string changes and creates more intricate folding to optimally pair opposite charges. The protein fold that is the final product represents the most stable pairing of positive and negative charges. Therefore, when it comes to human disease that arise from amino acid mutations in the string, this disrupts how the protein would normally fold and results in a unstable protein that would then either not do the job its supposed to do or get thrown to the garbage can of the cell. Apologies for the lengthy explanation!
If AI could design custom medicines just for you, firstly would you trust it? Secondly, what kind of breakthrough would you hope it solves (i.e. cancer, aging, rare diseases, or something else)?
This is the kind of news that needs to go viral.
"To a jelly fish we all look the same" - Neil Tyson
Look at Chuck bringing the real questions!
Chuck is self deprecating, but has some of the best insights and questions of anyone out there.
When I was a kid, my dad was a chemist and he DID come home smelling like chemicals. My mom would make him undress in the garage after he came home and out his clothes directly in the closet. He worked on acetaminophen.