The human insulin receptor substrate- 1 (IRS-1) is designated protein \(\mathrm{P} 35568\) in the protein knowledge base on the ExPASy Web site (http://us.expasy.org/). Go to the PeptideMass tool on this Web site and use it to see the results of trypsin digestion of IRS-1. How many amino acids does IRS-1 have? What is the average molecular mass of IRS-1? What is the amino acid sequence of the tryptic peptide of IRS-1 that has a mass of \(1741.9629 ?\)

Short Answer

Expert verified
The precise figures can only be obtained directly from the PeptideMass tool based on real time data, but the steps outlined would guide you to find the needed information about the human insulin receptor substrate-1 (IRS-1).

Step by step solution

01

Access the ExPASy Website

First, go to the ExPASy website at (http://us.expasy.org/). Here you'll find a wide range of tools for protein and gene analysis.
02

Find the IRS-1 Protein

Once on the website, you need to look up the IRS-1 protein, which is designated as P35568 in the Protein Knowledge Base. There is usually a search field on the webpage where you can input P35568 to search.
03

Use the PeptideMass Tool

From the protein page for IRS-1 (P35568) you will find an option to access the PeptideMass tool. This tool will allow you to see the results of trypsin digestion of IRS-1.
04

Interpret the Results

From the results provided by the PeptideMass tool, you will be able to find the number of amino acids in IRS-1, its average molecular mass, and the amino acid sequence of the tryptic peptide of IRS-1 that has a mass of 1741.9629.

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Key Concepts

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

ExPASy PeptideMass Tool
Understanding the fundamentals of biochemistry often involves knowing the details about proteins, such as their structure and mass. The ExPASy PeptideMass tool is a critical resource for researchers and students alike. This online tool, available on the ExPASy (Expert Protein Analysis System) website, allows users to compute the molecular mass of peptides.

This user-friendly tool requires the protein's unique identifier, like the IRS-1 protein's designated P35568. Once provided, the tool simulates an in-silico digestion using the specified enzyme, such as trypsin, and outputs a list of potential peptides along with their molecular masses. The trypsin digestion of IRS-1, for example, would produce a list of fragments that result from trypsin cutting at specific points in the amino acid sequence. Trypsin primarily cuts at the carboxyl side of the amino acids lysine and arginine, which provides a predictable pattern of fragmentation. This is instrumental in understanding the structural and functional aspects of proteins like IRS-1.
Amino Acid Sequence
The amino acid sequence is the order in which amino acids are linked together to form a protein. Each protein is unique because of their sequence of amino acids that determines its structure and function. Knowing the sequence of a protein, such as IRS-1, is crucial for many experimental procedures, including mass spectrometry.

When we look at the IRS-1 protein and its tryptic peptides, understanding the precise amino acid sequences aids researchers in identifying exact fragments generated by trypsin digestion. As observed in the ExPASy PeptideMass tool results, each fragment's sequence helps in deducing the protein's functionality and interaction with other molecules. It's like having a specific code to a lock; with the correct sequence, a scientist can unlock information about the protein's role and behavior in the body.
Molecular Mass Calculation
The molecular mass calculation is a fundamental concept in biochemistry, especially when discussing proteins and peptides. Molecular mass refers to the sum of the masses of all the atoms in a molecule. For proteins and peptides, this translates to the combined mass of all its constituent amino acids, typically measured in Daltons (Da) or atomic mass units (amu).

In the context of the IRS-1 protein, using a tool like ExPASy PeptideMass, the molecular mass calculation becomes more accessible. Once the tool has predicted the peptides generated by trypsin digestion, it calculates the mass of each peptide based on the known masses of the included amino acids. This mass is essential for experimental procedures such as mass spectrometry, where peptides are identified based on their mass-to-charge ratio. For example, the peptide of IRS-1 with a mass of 1741.9629 Da can be pinpointed and analyzed further to determine its role in the function of the protein.

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Most popular questions from this chapter

Proteases such as trypsin and chymotrypsin cleave proteins at different sites, but both use the same reaction mechanism. Based on your knowledge of organic chemistry, suggest a "universal" protease reaction mechanism for hydrolysis of the peptide bond.

Describe the synthesis of the dipeptide Lys-Ala by Merrifield's solidphase chemical method of peptide synthesis. What pitfalls might be encountered if you attempted to add a leucine residue to Lys-Ala to make a tripeptide?

Amino acid analysis of a decapeptide revealed the presence of the following products: \(\begin{array}{lllll}\mathrm{NH}_{4}^{+} & \text {Asp } & \text { Glu } & \text { Tyr } & \text { Arg } \\ \text { Met } & \text { Pro } & \text { Lys } & \text { Ser } & \text { Phe }\end{array}\) The following facts were observed: a. Neither carboxypeptidase \(A\) or \(B\) treatment of the decapeptide had any effect. b. Trypsin treatment yielded two tetrapeptides and free Lys. c. Clostripain treatment yielded a tetrapeptide and a hexapeptide. d. Cyanogen bromide treatment yielded an octapeptide and a dipeptide of sequence NP (using the one-letter codes). e. Chymotrypsin treatment yielded two tripeptides and a tetrapeptide. The N-terminal chymotryptic peptide had a net charge of -1 at neutral \(\mathrm{pH}\) and a net charge of -3 at pH 12 f. One cycle of Edman degradation gave the PTH derivative What is the amino acid sequence of this decapeptide?

Phosphoproteins are formed when a phosphate group is esterified to an - OH group of a Ser, Thr, or Tyr side chain. At typical cellular \(\mathrm{pH}\) values, this phosphate group bears two negative charges \(-\mathrm{OPO}_{3}^{2-} .\) Compare this side-chain modification to the 20 side chains of the common amino acids found in proteins and comment on the novel properties that it introduces into side-chain possibilities.

Amino acid analysis of an octapeptide revealed the following composition: \(\begin{array}{llllll}\text { 2 Arg } & \text { 1 Gly } & \text { 1 Met } & \text { 1 Trp } & \text { 1 Tyr } & \text { 1 Phe } & \text { 1 Lys }\end{array}\) The following facts were observed: a. Edman degradation gave b. CNBr treatment yielded a pentapeptide and a tripeptide containing phenylalanine. c. Chymotrypsin treatment yielded a tetrapeptide containing a C-terminal indole amino acid and two dipeptides. d. Trypsin treatment yielded a tetrapeptide, a dipeptide, and free Lys and Phe. e. Clostripain yielded a pentapeptide, a dipeptide, and free Phe. What is the amino acid sequence of this octapeptide?

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