Great video! my question is, how do we determine which amino acid is more hydrophobic or hydrophilic than another by just looking at its structure. An example being isoleucine is more hydrophobic than phenylalanine.
@TheMCATTutorr
Жыл бұрын
Hi Audrey! Thanks for the comment. Amino acids with non-polar, hydrophobic side chains (such as alanine, valine, leucine, and isoleucine) tend to be hydrophobic. They tend to aggregate and avoid contact with water. On the other hand, amino acids with polar or charged side chains (such as asparagine, glutamine, lysine, arginine, and phenylalanine) tend to be hydrophilic and interact well with water. The relative hydrophobicity or hydrophilicity of an amino acid can be further refined by looking at the length, shape, and charge of its side chain. In general, longer, more flexible, and more highly charged side chains tend to be more hydrophilic, while shorter, more rigid, and more hydrophobic side chains tend to be more hydrophobic. I hope this helps!
@annietembo-os7ze
Жыл бұрын
Wonderful video, my question is how can I make the table of 20 drawings of amino acids with their hydrophobic, hydrophilic, basic and acidic?
@TheMCATTutorr
Жыл бұрын
Hi! I'm glad the video was helpful for you! Hmm.. I see how a table with those categories could help. I would pretty much follow a similar format to this video: kzitem.info/news/bejne/r6WwmImGsmJ6lZg However, I will probably start working on a video for this :) I was also wondering, would you be interested if I made those tables and link it to the channel so students could download them?
@tzvigreenberg443
2 жыл бұрын
Jack Westing has it flipped, Cysteine is Polar while Tyrosine is non-polar, any idea why?
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