/*! This file is auto-generated */ .wp-block-button__link{color:#fff;background-color:#32373c;border-radius:9999px;box-shadow:none;text-decoration:none;padding:calc(.667em + 2px) calc(1.333em + 2px);font-size:1.125em}.wp-block-file__button{background:#32373c;color:#fff;text-decoration:none} Problem 23 You have isolated a tripeptide c... [FREE SOLUTION] | 91Ó°ÊÓ

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You have isolated a tripeptide containing Arg, His, and Pro. How many different sequences are possible for this tripeptide?

Short Answer

Expert verified
There are 6 possible sequences for the tripeptide Arg-His-Pro.

Step by step solution

01

Understanding the Problem

We need to determine the number of different sequences that can be formed by the tripeptide made of amino acids Arginine (Arg), Histidine (His), and Proline (Pro). This is a permutation problem where the order of the amino acids matters.
02

Identify the Total Number of Amino Acids

Since we are dealing with a tripeptide, there are three amino acids: Arg, His, and Pro.
03

Calculate Factorial of Total Amino Acids

To find all possible sequences, calculate the factorial of the number of amino acids. This is because we are arranging all of the amino acids, and no repetitions are allowed. Thus, we calculate: \[3! = 3 \times 2 \times 1 = 6\]
04

List Possible Sequences (Optional Verification)

To verify, list all permutations of Arg, His, and Pro: 1. Arg-His-Pro 2. Arg-Pro-His 3. His-Arg-Pro 4. His-Pro-Arg 5. Pro-Arg-His 6. Pro-His-Arg. This confirms there are indeed 6 sequences.

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Key Concepts

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

Amino Acids
Amino acids are the fundamental building blocks of proteins. Proteins are essential macromolecules for all living organisms. Each amino acid consists of a central carbon atom bonded to four different groups: an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom, and a distinctive side chain. This side chain varies among different amino acids, giving each one unique properties.
  • Arginine (Arg) has a positively charged side chain, making it basic. It's often involved in the formation of protein structures.
  • Histidine (His) also has a basic side chain and can both donate and accept protons, making it critical in enzyme active sites.
  • Proline (Pro) is unique because its side chain links back to the amino group, forming a cyclic structure that influences the folding of proteins.
Understanding the unique characteristics of each amino acid helps in grasping how proteins are structured and function.
Permutation
In mathematics, permutation refers to the arrangement of all the members of a set into some sequence or order. Specifically, it deals with arranging objects where order matters. In this tripeptide problem, permutation is key because the sequence in which amino acids are arranged defines the identity and function of the resulting peptide.
When dealing with a permutation, we consider all possible ways to order the elements in a sequence. For example, with three distinct amino acids—Arg, His, and Pro—we want to find all unique sequences in which these can be arranged.
To calculate the number of permutations, one often applies a factorial function. This is expressed as 3! (3 factorial) because we have three unique items (amino acids) to arrange. Calculating this gives:\[3! = 3 \times 2 \times 1 = 6\]
This mathematical concept underpins many biological and chemical processes where the arrangement of components determines function.
Tripeptide
A tripeptide is a specific type of peptide composed of three amino acids linked together by peptide bonds. The sequence of these amino acids imparts distinct structural and functional characteristics to the peptide.
Peptides are formed when the amino group of one amino acid reacts with the carboxyl group of another, releasing a water molecule in a process known as condensation.
For the amino acids Arg, His, and Pro, the tripeptide can have different sequences:
  • Arg-His-Pro
  • Arg-Pro-His
  • His-Arg-Pro
  • His-Pro-Arg
  • Pro-Arg-His
  • Pro-His-Arg
Each of these sequences represents a unique tripeptide, underscoring the importance of amino acid order. This order can significantly affect the structure and biological activity of the peptide, demonstrating how vital permutation is in biochemical reactions.

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Most popular questions from this chapter

Rank the solubility of the following amino acids in water at \(\mathrm{pH} 7\) : Trp, Arg, Ser, Val, Thr.

Proteins can be unfolded, or denatured, by agents that alter the balance of weak noncovalent forces that maintain the native conformation. How would the following agents cause a protein to denature? Be specific about the type of intermolecular forces that would be affected. a. Heat; b. \(\mathrm{pH}\); c. amphiphilic detergents; d. reducing agents such as 2 -mercaptoethanol ( \(\left.\mathrm{HSCH}_{2} \mathrm{CH}_{2} \mathrm{OH}\right)\).

The \(p K\) values of the amino and carboxylate groups in free amino acids differ from the \(\mathrm{p} K\) values of the \(\mathrm{N}\) - and C-termini of polypeptides. Explain.

A protein engineering laboratory studying monoclonal antibody proteins characterized the thermal stability of these proteins by measuring their melting temperature \(\left(T_{\mathrm{m}}\right)\), defined as the temperature at which the proteins are half unfolded. The investigators found a positive correlation between \(T_{\mathrm{m}}\) and the proteins' - SH content. In other words, proteins with more \(-\mathrm{SH}\) groups were more thermally stable. Explain this observation.

In structural studies of a staphylococcal nuclease enzyme, a valine residue buried in the protein's interior was experimentally changed, first to an Asp residue, and then, in a second experiment, to a Lys residue. How do the \(\mathrm{p} K\) values of the a. Asp and b. Lys residues in the mutant nucleases compare to those listed for the free amino acids in Table 4.1?

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