Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Chapter 5, Problem 42RE
Interpretation Introduction
Interpretation:
By a series of equations (with structures) the first stage of the Edman method applied to a peptide that has a leucine as its N-terminal residue, is to be shown.
Concept introduction:
Edman degradation is one of the methods used for elucidating the sequence of amino acids present in the peptides of the protein, which is being studied.
Leucine is an
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Chapter 5 Solutions
Biochemistry
Ch. 5 - RECALL What types of homogenization techniques are...Ch. 5 - RECALL When would you choose to use a...Ch. 5 - RECALL What is meant by salting out? How does it...Ch. 5 - RECALL What differences between proteins are...Ch. 5 - RECALL How could you isolate mitochondria from...Ch. 5 - RECALL Can you separate mitochondria from...Ch. 5 - RECALL Give an example of a scenario in which you...Ch. 5 - Prob. 8RECh. 5 - REFLECT AND APPLY You are purifying a protein for...Ch. 5 - Prob. 10RE
Ch. 5 - RECALL What is the basis for the separation of...Ch. 5 - RECALL What is the order of elution of proteins on...Ch. 5 - RECALL What are two ways that a compound can be...Ch. 5 - Prob. 14RECh. 5 - RECALL Why do most people elute bound proteins...Ch. 5 - RECALL What are two types of compounds that make...Ch. 5 - RECALL Draw an example of a compound that would...Ch. 5 - RECALL How can gel-filtration chromatography be...Ch. 5 - REFLECT AND APPLY Sephadex G-75 has an exclusion...Ch. 5 - Prob. 20RECh. 5 - RECALL What is the main difference between reverse...Ch. 5 - RECALL How does HPLC differ from ion-exchange...Ch. 5 - REFLECT AND APPLY Design an experiment to purify...Ch. 5 - REFLECT AND APPLY Referring to Question 23, how...Ch. 5 - Prob. 25RECh. 5 - REFLECT AND APPLY You wish to separate and purify...Ch. 5 - REFLECT AND APPLY An amino acid mixture consisting...Ch. 5 - REFLECT AND APPLY An amino acid mixture consisting...Ch. 5 - REFLECT AND APPLY In reverse-phase HPLC, the...Ch. 5 - REFLECT AND APPLY Gel-filtration chromatography is...Ch. 5 - RECALL What physical parameters of a protein...Ch. 5 - RECALL What types of compounds make up the gels...Ch. 5 - RECALL Of the two principal polymers used in...Ch. 5 - RECALL What types of macromolecules are usually...Ch. 5 - RECALL If you had a mixture of proteins with...Ch. 5 - RECALL What does SDSPAGE stand for? What is the...Ch. 5 - RECALL How does the addition of sodium...Ch. 5 - RECALL Why is the order of separation based on...Ch. 5 - RECALL The accompanying figure is from an...Ch. 5 - Prob. 40RECh. 5 - Prob. 41RECh. 5 - Prob. 42RECh. 5 - Prob. 43RECh. 5 - REFLECT AND APPLY What would happen during an...Ch. 5 - REFLECT AND APPLY A sample of an unknown peptide...Ch. 5 - REFLECT AND APPLY A sample of a peptide of unknown...Ch. 5 - REFLECT AND APPLY You are in the process of...Ch. 5 - REFLECT AND APPLY You are in the process of...Ch. 5 - Prob. 49RECh. 5 - Prob. 50RECh. 5 - Prob. 51RECh. 5 - Prob. 52RECh. 5 - Prob. 53RECh. 5 - Prob. 54RECh. 5 - RECALL What is the basis for the technique called...Ch. 5 - Prob. 56RECh. 5 - Prob. 57RECh. 5 - RECALL What are the main procedures involved in a...Ch. 5 - RECALL Where did western blot get its name?Ch. 5 - Prob. 60RECh. 5 - Prob. 61RECh. 5 - Prob. 62RECh. 5 - Prob. 63RECh. 5 - Prob. 64RECh. 5 - Prob. 65RE
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- REFLECT AND APPLY Explain why a 50S ribosomal subunit and a 30S ribosomal subunit combine to form a 70S subunit, instead of an 80S subunit.arrow_forwardREFLECT AND APPLY You are in the process of determining the amino acid sequence of a peptide. After trypsin digestion followed by the Edman degradation, you see the following peptide fragments: LeuGlyArgGlySerPheTyrAsnHisSerGluAspMetCysLysThrTyrGluValCysMetHis What is abnormal concerning these results? What might have been the problem that caused it?arrow_forwardREFLECT AND APPLY A sample of an unknown peptide was divided into two aliquots. One aliquot was treated with trypsin; the other was treated with cyanogen bromide. Given the following sequences (N-terminal to C-terminal) of the resulting fragments, deduce the sequence of the original peptide. Trypsin treatment AsnThrTrpMetIleLysGlyTyrMetGlnPheValLeuGlyMetSerArg Cyanogen bromide treatment GlnPheValLeuGlyMetIleLysGlyTyrMetSerArgAsnThrTrpMetarrow_forward
- REFLECT AND APPLY Why is a trimming process important in converting precursors of tRNA and rRNA to the active forms?arrow_forwardREFLECT AND APPLY You are in the process of determining the amino acid sequence of a protein and must reconcile contradictory results. In one trial, you determine a sequence with glycine as the N-terminal amino acid and asparagine as the C-terminal amino acid. In another trial, your results indicate phenylalanine as the N-terminal amino acid and alanine as the C-terminal amino acid. How do you reconcile this apparent contradiction?arrow_forwardREFLECT AND APPLY A sample of a peptide of unknown sequence was treated with trypsin; another sample of the same peptide was treated with chymotrypsin. The sequences (N-terminal to C-terminal) of the smaller peptides produced by trypsin digestion were as follows: MetValSerThrLysValIleTrpThrLeuMetIleLeuPheAsnGluSeArg The sequences of the smaller peptides produced by chymotrypsin digestion were as follows: AsnGluSerArgValIleTrpThrLeuMetIleMetValSerThrLysLeuPhe Deduce the sequence of the original peptide.arrow_forward
- REFLECT AND APPLY E. coli incorporates deoxyribonucleotides into DNA at a rate of 250 to 1000 bases per second. Using the higher value, translate this into typing speed in words per minute. (Assume five characters per word, using the typing analogy from Question 36.)arrow_forwardREFLECT AND APPLY The fidelity of protein synthesis is assured twice during protein synthesis. How and when?arrow_forwardREFLECT AND APPLY It is possible for the codons for a single amino acid to have the first two bases in common and to differ in the third base. Why is this experimental observation consistent with the concept of wobble?arrow_forward
- REFLECT AND APPLY The enzyme D-amino acid oxidase has a very high turnover number because the D-amino acids are potentially toxic. The KM for the enzyme is in the range of 1 to 2 mM for the aromatic amino acids and in the range of 15 to 20 mM for such amino acids as serine, alanine, and the acidic amino acids. Which of these amino acids are the preferred substrates for the enzyme?arrow_forwardREFLECT AND APPLY Suggest an explanation for the observation that when proteins are chemically modified so that specific side chains have a different chemical nature, these proteins cannot be denatured reversibly.arrow_forwardREFLECT AND APPLY The amino acid hydroxyproline is found in collagen. There is no codon for hydroxyproline. Explain the occurrence of this amino acid in a common protein.arrow_forward
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