Question

In: Chemistry

Which amino acid is the most hydrophobic? (1pt) Arginine Aspartic Acid Leucine Serine Tyrosine

Which amino acid is the most hydrophobic? (1pt)

Arginine

Aspartic Acid

Leucine

Serine

Tyrosine

Solutions

Expert Solution

LEUCINE is most hydrophobic among these amino acids.

Most protein molecules have a hydrophobic core, which is not accessible to solvent and a polar surface in contact with the environment (although membrane proteins follow a different pattern). While hydrophobic amino acid residues build up the core, polar and charged amino acids preferentially cover the surface of the molecule and are in contact with solvent due to their ability to form hydrogen bonds.

Hydrophobic amino acids are mostly buried within the core of the structure, a smaller fraction of polar groups are found to be buried. Charged residues are exposed to solvent to a much higher degree.


Related Solutions

1.The amino acid serine is classified as a(n) _________________________________________________ amino acid. 2.A type of chromatography that...
1.The amino acid serine is classified as a(n) _________________________________________________ amino acid. 2.A type of chromatography that fractionates proteins based on differences in their size is ____________________________________ chromatography. 3. In Anfinsen's experiments on the structure and function of RNase, he found that non-covalent bonds were key in determining the _________________________ structure of the enzyme. 4. A type of reversible enzyme inhibitor that binds to the active site of an enzyme and prevents the substrate from binding the active site is is...
6. A bacterium does not want to waste energy synthesizing the amino acid arginine if arginine...
6. A bacterium does not want to waste energy synthesizing the amino acid arginine if arginine is present in its diet. Therefore, when arginine is present, it activates a repressor protein to prevent transcription of genes that code for enzyme to make arginine. This is an example of what type of regulation? Please describe the mechanism of this regulation. 7. Prokaryotic genetic information transferring processusually acts as target of antibiotics. We observed a new compound with antibiotic action, and we...
Consider a 0.487 L solution of the amino aspartic acid (0.685 M), which ahs a carboxylic...
Consider a 0.487 L solution of the amino aspartic acid (0.685 M), which ahs a carboxylic acid group (pKa = 2.10), an amine group (pKa = 9.82), and a carboxylic acid side chain (pKa = 3.86). How many liters of 2.59 M NaOH would you need to add to reach the isoelectric point of the amino acid?
You have accidentally mixed a bunch of amino acids (tryptophan, tyrosine, alanine, selenocysteine, proline, arginine) together...
You have accidentally mixed a bunch of amino acids (tryptophan, tyrosine, alanine, selenocysteine, proline, arginine) together and once your boss finds out, you will be fired on the spot. Your only hope of saving your job is to separate them before anyone finds out. You decide that the only viable option is to use ion exchange chromatography. Explain, in detail, how you would do this?
Determine the isoelectric pH for threonine, aspartic acid, arginine, and the tripeptide his-ile-lys. You will probably...
Determine the isoelectric pH for threonine, aspartic acid, arginine, and the tripeptide his-ile-lys. You will probably have to write out the equations in order to do this correctly.
A mutation replaces the original amino acid, leucine, with threonine in a large protein. The altered...
A mutation replaces the original amino acid, leucine, with threonine in a large protein. The altered protein still functions, but less efficiently. What amino acid might replace leucine but with less effect on protein functions? What amino acid might replace leucine but with even a worse effect on the how the protein functions? a) less effect if lysine; worse if alanine b) less effect if methionine; worse if lysine c) less effect if methionine; worse if alanine d) less effect...
The amino acid leucine has two titratable groups, the α-amino, pKa 9.6 and the α-carboxyl, pKa...
The amino acid leucine has two titratable groups, the α-amino, pKa 9.6 and the α-carboxyl, pKa 2.4. Calculate the ratio of acidic and basic forms and express them as [A]/[HA] ratio or [B]/[BH] of the titrating group at the following pH values: α-carboxyl @ 1.4, 1.9, 2.4, 2.9, 3.4; α-amino @ 8.1, 8.6, 9.1, 9.6, 10.1. Plot pH vs. [B]/[BH] for each group, on the same graph. Compare similarities or disparities in the titration of each group.
Question 2 Tyrosine is a triprotic amino acid with pKa of 2.17, 9.19, and 10.47 The...
Question 2 Tyrosine is a triprotic amino acid with pKa of 2.17, 9.19, and 10.47 The first proton is removed from the carboxylic acid ( –COOH), the second from the protonated amine group (–NH3 +) . The third, with a pKa of 10.47, is the phenolic proton (–OH) on the aromatic ring. Tyrosine a) What is the structure of the most protonated form of tyrosine in aqueous solution? ! "#$%!*!'(!)! b) Write the three acid dissociation equilibria with the correct...
L-Serine is an amino acid that often is provided when intravenous feeding solutions are used to...
L-Serine is an amino acid that often is provided when intravenous feeding solutions are used to maintain the health of a patient. Molecular weight of 105, produced by fermentation and recovered and purified by crystallization at 10C. Yield is enhanced by adding methanol to the system, thereby reducing serine solubility in aqueous solutions. An aqueous serine solution containing 30wt% serine and 70wt% water is added along with methanol to a batch crystallizer thatis allowed to equilibrate at 10C. The resulting...
Which of these amino acids doesn't fit with the others? Alanine Glycine Serine Proline
Which of these amino acids doesn't fit with the others? Alanine Glycine Serine Proline
ADVERTISEMENT
ADVERTISEMENT
ADVERTISEMENT