Identify each of these supersecondary motifs! Sorry about the size of the images...
Protein Modeling C
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EwwPhysics
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Protein Modeling C
Let's get this one started! Starting out with an easy question...
Identify each of these supersecondary motifs! Sorry about the size of the images...
Identify each of these supersecondary motifs! Sorry about the size of the images...
Last edited by EwwPhysics on October 13th, 2020, 9:05 am, edited 2 times in total.
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azboy1910
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Re: Protein Modeling C
Don't know if these answers are correct, but here goes nothing . . .
I believe the first one is a beta-alpha-beta motif, the second one is a greek key motif, and the bottom one is a beta barrel.
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EwwPhysics
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Re: Protein Modeling C
Good job!
1.
Zinc finger motif
Correct!
Correct!
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Ninn
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Re: Protein Modeling C
1. Why is glycine commonly found in protein linkers?
2. Arginine, histidine, and lysine are all positively charged, but what makes histidine the best buffer of these three?
3. Is aspartic acid or glutamic acid more acidic, and why?
2. Arginine, histidine, and lysine are all positively charged, but what makes histidine the best buffer of these three?
3. Is aspartic acid or glutamic acid more acidic, and why?
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popcorn3
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Re: Protein Modeling C
Fun questions!
1. Glycine is a very "flexible" residue due to its very small sidechain (just a hydrogen). This means the domains/proteins that the linkers connect can move around and interact with each other. 2. Histidine has the pKa closest to physiological pH, so it best acts as a buffer in biological systems. 3. Aspartic acid is more acidic. Couldn't tell you why, but my guess is induction effects, since the only difference between Asp and Glu is the sidechain's distance from the NH2 group.
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Ninn
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Re: Protein Modeling C
All correct! You're right regarding induction for #3 too -- the additional methylene of Glu weakens its inductive effect. The stronger the inductive effect the more acidic the compound, so like you said, Asp is more acidic :)popcorn3 wrote: ↑April 3rd, 2021, 10:34 am Fun questions!1. Glycine is a very "flexible" residue due to its very small sidechain (just a hydrogen). This means the domains/proteins that the linkers connect can move around and interact with each other. 2. Histidine has the pKa closest to physiological pH, so it best acts as a buffer in biological systems. 3. Aspartic acid is more acidic. Couldn't tell you why, but my guess is induction effects, since the only difference between Asp and Glu is the sidechain's distance from the NH2 group.
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