Jump to content

Why is Sheldon's Favorite Aminoacid Lysine?


Recommended Posts

Is there any reason for that?

Pappa Wiki says.....

Lysine (abbreviated as Lys or K)[2] is an α-amino acid with the chemical formula HO2CCH(NH2)(CH2)4NH2. It is an essential amino acid, which means that the human body cannot synthesize it. Lysine's codons are AAA and AAG.

Lysine is a base, as are arginine and histidine. The ε-amino group often participates in hydrogen bonding and as a general base in catalysis. (The ε-amino group, which is attached to the NH3+ group, is the fifth carbon down from the α-carbon, which is attached to the carboxyl (C=OOH) group.[3])

Common posttranslational modifications include methylation of the ε-amino group, giving methyl-, dimethyl-, and trimethyllysine. The latter occurs in calmodulin. Other posttranslational modifications at lysine residues include acetylation and ubiquitination. Collagen contains hydroxylysine, which is derived from lysine by lysyl hydroxylase. O-Glycosylation of hydroxylysine residues in the endoplasmic reticulum or Golgi apparatus is used to mark certain proteins for secretion from the cell.

So your guess is as good as mine here.....

Share this post


Link to post
Share on other sites

Is there any reason for that?

Pappa Wiki says.....

Lysine (abbreviated as Lys or K)[2] is an α-amino acid with the chemical formula HO2CCH(NH2)(CH2)4NH2. It is an essential amino acid, which means that the human body cannot synthesize it. Lysine's codons are AAA and AAG.

Lysine is a base, as are arginine and histidine. The ε-amino group often participates in hydrogen bonding and as a general base in catalysis. (The ε-amino group, which is attached to the NH3+ group, is the fifth carbon down from the α-carbon, which is attached to the carboxyl (C=OOH) group.[3])

Common posttranslational modifications include methylation of the ε-amino group, giving methyl-, dimethyl-, and trimethyllysine. The latter occurs in calmodulin. Other posttranslational modifications at lysine residues include acetylation and ubiquitination. Collagen contains hydroxylysine, which is derived from lysine by lysyl hydroxylase. O-Glycosylation of hydroxylysine residues in the endoplasmic reticulum or Golgi apparatus is used to mark certain proteins for secretion from the cell.

So your guess is as good as mine here.....

As Penny would say: What???

Share this post


Link to post
Share on other sites

My thought is that it is his favorite because it was mentioned in the Jurassic Park movie.

I never did understand the Lysine Contingency from Jurassic Park. Animals can't produce lysine to begin with, so I'm not sure what exactly Henry's character was thinking.

As far as Sheldon goes, he seems to view -as part of his more evolved status- human contact as repulsive and unnecessary. He may see the STD-treatment aspect of lysine as some sort of vindication... it's reachin' but it's all I got - lol.

Share this post


Link to post
Share on other sites
  • 5 years later...

Okay, here's my two cents' worth... Lysine has an unusual chemical structure. It has a long (four-carbon) side chain terminating in just a little amino group. All other amino acids have side chains which are shorter, wider, or both. 

So of course Sheldon likes Lysine. It's long, skinny and unique (as he sees it) or weird (the rest of us).  It's just like him.

 

300px-L-Lysin_-_L-Lysine_svg.png.6b5ffb4bbfb98c6cb6d404fc2dbdfcb0.png

Share this post


Link to post
Share on other sites

Join the conversation

You can post now and register later. If you have an account, sign in now to post with your account.
Note: Your post will require moderator approval before it will be visible.

Guest
Reply to this topic...

×   Pasted as rich text.   Paste as plain text instead

  Only 75 emoji are allowed.

×   Your link has been automatically embedded.   Display as a link instead

×   Your previous content has been restored.   Clear editor

×   You cannot paste images directly. Upload or insert images from URL.

×
×
  • Create New...

Important Information

We have placed cookies on your device to help make this website better. You can adjust your cookie settings, otherwise we'll assume you're okay to continue.