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Chapter 5: Q14CP (page 119)

What types of information can be retrieved from a protein sequence database?

Short Answer

Expert verified

The protein sequence database retrieve protein sequence records by gene name, organism, author name, accession number and a variety of other text terms.

Step by step solution

01

Protein database

Protein databaseis a collection of sequences from several sources, including translations from annotated coding regions in GenBank. They are an important resource because proteins mediate most biological functions.

02

SWISS-PROT database

It is acurated protein sequence database which strives to provide a high level of annotations like protein function, domain structure, modifications observed after translation, variants and so on.

03

Accuracy

A minimal level of repetition and high level of integration with other database.

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Most popular questions from this chapter

What fractionation procedure could be used to purify protein 1 from a mixture of three proteins whose amino acid compositions are as follows?

1. 25% Ala, 20% Gly, 20% Ser, 10% Ile, 10% Val, 5% Asn, 5% Gln, 5% Pro

2. 30% Gln, 25% Glu, 20% Lys, 15% Ser, 10% Cys

3. 25% Asn, 20% Gly, 20% Asp, 20% Ser, 10% Lys, 5% Tyr

All three proteins are similar in size and pI, and there is no antibody available for protein 1.

You are using ammonium sulphate to purify protein Q (pI = 5.0) by salting out from a solution at pH 7.0. How should you adjust the pH of the mixture to maximize the amount of protein Q that precipitates?

You must cleave the following peptide into smaller fragments. Which of the proteases listed in Table 5-4 would be likely to yield the most fragments? The fewest?

NMTQGRCKPVNTFVHEPLVDVQNVCFKE

Explain how you would use salting out to prepare a more concentrated solution of a protein.

You wish to determine the sequence of a polypeptide that has the following amino acid composition.

1 Ala 4 Arg 2 Asn 3 Asp 4 Cys 3 Gly 1 Gln 4 Glu 1 His 1 Lys 1 Met 1 Phe 2 Pro 4 Ser 2 Tyr 1 Trp

(a) What is the maximum number of peptides you can expect if you cleave the polypeptide with cyanogen bromide?

(b) What is the maximum number of peptides you can expect if you cleave the polypeptide with chymotrypsin?

(c) Analysis of the intact polypeptide reveals that there are no free sulfhydryl groups. How many disulfide bonds are likely to be present?

(d) How many different arrangements of disulfide bonds are possible?
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