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How many different tripeptides can be formed by lysine and alanine?

Short Answer

Expert verified
The number of different tripeptides that can be formed by lysine and alanine is 8.

Step by step solution

01

Understanding Permutations

Permutations refer to the arrangement of items where the order of selection matters. In this instance, each position in the tripeptide (3 positions) can be occupied by either lysine or alanine.
02

Calculating Permutations

When calculating permutations with repetition allowed, the formula is \(n^r\), where \(n\) is the number of options for each position and \(r\) is the number of positions. In this case, \(n = 2\) (lysine, alanine) and \(r = 3\) (3 positions in the tripeptide). Plug in these values to the formula \((2)^3\).
03

Final Calculation

The final calculation is \(2^3 = 8\). Therefore, there are eight different tripeptides which can be formed by lysine and alanine.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Tripeptides Formation
The process of forming tripeptides involves joining three amino acids in a specific sequence. Peptides are short chains of amino acids linked by peptide bonds, and tripeptides, as the name suggests, are composed of three such units. In biochemistry, the order of amino acids in a peptide chain is crucial, as it determines the peptide's properties and function.

When considering tripeptides composed of only two types of amino acids, such as lysine and alanine, the possible permutations of these amino acids dictate the different tripeptides that can be created. Each of the three positions in the tripeptide can be occupied by either amino acid, resulting in a variety of combinations. This variety is important for biological diversity since even small changes in the peptide sequence can have significant effects on how the molecule interacts with others in the body.
Amino Acids Permutations
To understand amino acids permutations, it's essential to grasp the concept of permutations in a broader sense. Permutations are various possible arrangements of a set of items where the order is important. Applying this concept to amino acids in a peptide chain, the number of permutations represents the different sequences in which the amino acids can appear.

For calculating permutations with repetition, the formula used is \(n^r\), where \(n\) is the number of amino acids to choose from, and \(r\) is the number of positions in the peptide. For the tripeptide example with lysine and alanine, each amino acid has the chance to be at any position in the peptide chain, leading to different sequences and thus, different peptides.
Lysine and Alanine
Lysine and alanine are two fundamentally different amino acids that play unique roles in biochemistry. Lysine is a basic, positively charged amino acid, often involved in protein structure, by forming ionic bonds and hydrogen bonds. Alanine, on the other hand, is a small, nonpolar amino acid that is often involved in the biosynthesis of proteins.

When considering peptides made of lysine and alanine, the properties of the resulting tripeptide will vary depending on the sequence of these amino acids. For example, a tripeptide with lysine at both ends might have different solubility or bonding properties compared to one with alanine at the ends. This variety in the chemical nature and sequence of amino acids is what allows for the diverse functionality of peptides and proteins in living organisms.

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Most popular questions from this chapter

In protein synthesis, the selection of a particular amino acid is determined by the so-called genetic code, or a sequence of three bases in DNA. Will a sequence of only two bases unambiguously determine the selection of 20 amino acids found in proteins? Explain.

When deoxyhemoglobin crystals are exposed to oxygen, they shatter. On the other hand, deoxymyoglobin crystals are unaffected by oxygen. Explain. (Myoglobin is made up of only one of the four subunits, or polypeptide chains, in hemoglobin.)

When a nonapeptide (containing nine amino acid residues) isolated from rat brains was hydrolyzed, it gave the following smaller peptides as identifiable products: Gly-Ala-Phe, Ala-Leu-Val, Gly-Ala-Leu, Phe-Glu-His, and His-Gly-Ala. Reconstruct the amino acid sequence in the nonapeptide, giving your reasons. (Remember the convention for writing peptides.)

Teflon is formed by a radical addition reaction involving the monomer tetrafluoroethylene. Show the mechanism for this reaction.

Molar mass measurements play an important role in characterizing polymer solutions. Number-average molar mass \(\left(\bar{M}_{n}\right)\) is defined as the total molar mass (given by \(\Sigma N_{i} M_{i}\) ) divided by the total number of molecules: $$ \bar{M}_{n}=\frac{\Sigma N_{i} M_{i}}{\Sigma N_{i}} $$ where \(N_{i}\) is the number of molecules with molar mass \(M_{i}\). Another important definition is the weightaverage molar mass \(\left(\bar{M}_{w}\right)\) where $$\bar{M}_{w}=\frac{\Sigma N_{i} M_{i}^{2}}{\Sigma N_{i} M_{i}}$$ The difference between these two definitions is that \(\bar{M}_{w}\) is based on experimental measurements that are affected by the size of molecules. (a) Consider a solution containing five molecules of molar masses \(1.0,3.0,4.0,4.0,\) and \(6.0 \mathrm{~kg} / \mathrm{mol} .\) Calculate both \(\bar{M}_{n}\) and \(\bar{M}_{w}\). (b) \(\bar{M}_{w}\) is always greater than \(\bar{M}_{n}\) because of the square term in the definition. However, if all the molecules have identical molar mass, then we have \(\bar{M}_{n}=\bar{M}_{w} .\) Show that this is the case if we have four molecules having the same molar mass of \(5 \mathrm{~kg} / \mathrm{mol} .\) (c) Explain how a comparison of these two average molar masses gives us information about the distribution of the size of synthetic polymers like polyethylene and poly(vinyl chloride). (d) Proteins like myoglobin and cytochrome \(c\) have the same \(\bar{M}_{n}\) and \(\bar{M}_{w},\) while this is not the case for hemoglobin. Explain.

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