9th Edition

ISBN: 9781337805100

Author: Campbell

Publisher: CENGAGE L

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We generally tend to think of proteins only from a dietary lens, as a component of what we eat. However, they are among the most important and abundant organic macromolecules in the human body, with diverse structures and functions. Every cell contains t…

Protein Expression

The method by which living organisms synthesize proteins and further modify and regulate them is called protein expression. Protein expression plays a significant role in several types of research and is highly utilized in molecular biology, biochemistry…

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Textbook Question

Chapter 17, Problem 36RE

REFLECT AND APPLLY What is the metabolic advantage in the conversion of glucose to lactate, in which there is no net oxidation or reduction?

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Chapter 17, Problem 35RE

Chapter 17, Problem 37RE

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Electrophoresis Macmillan Learning Chymotrypsin is a protease with a molecular mass of 25.6 kDa. The figure shows a stained SDS polyacrylamide gel with a single band in lane I and three bands of lower molecular weight in lane 2. Lane I contains a preparation of chymotrypsin and lane 2 contains chymotrypsin pre-treated with performic acid. 1 2 Why does performic acid treatment of chymotrypsin generate three bands in lane 2? ° Chymotrypsin self-digests on the carboxyl-terminal side of phenylalanine, tryptophan, or tyrosine residues. The three peptides are impurities in the original chymotrypsin sample. Performic acid cleaves proteins on the carboxyl-terminal side of lysine and arginine residues. Performic acid cleaves the disulfide bonds holding together the three subunits of chymotrypsin. Correct Answer

Extracts from the bacterium Bacillus brevis contain a peptide with antibiotic properties. This peptide forms complexes with metal ions and seems to disrupt ion transport across the cell membranes of other bacterial species, leading to bacterial death. The structure of the peptide has been determined from a series of observations. (a) Complete acid hydrolysis of the peptide, followed by amino acid analysis, yielded equimolar amounts of Leu, Orn, Phe, Pro, and Val. Orn is ornithine, an amino acid not present in proteins but present in some peptides. Orn has the structure H 'H,N-CH, - CH2 CH2 CH2 - C - COO- NH, (b) The molecular weight of the peptide is approximately 1,200 Da. (c) The peptide failed to undergo hydrolysis when treated with the enzyme carboxypeptidase. This enzyme catalyzes the hydrolysis of the carboxyl-terminal residue of a polypeptide unless the residue is Pro or the peptide does not contain a free carboxyl group. (d) Treatment of the intact peptide with…

At a pH equal to the isoelectric point (pl) of alanine, the net charge of alanine is zero. Two structures can be drawn that have a net charge of zero, but the predominant form of alanine at its pl is zwitterionic. CH3 H,N CH3 ** H¸N-C H Zwitterionic H Uncharged OH Select statements that explain why alanine is predominantly zwitterionic at its pl. pk of alanine's amino group is more than its pl. pk of alanine's carboxyl group is more than its pl. PK of alanine's carboxyl group is less than its pl. pk of alanine's amino group is less than its pl. Correct Answer What fraction of alanine is in the completely uncharged form at its pl? 1 in 2.2 × 107 1 in 1.6 × 10² 1 in 4680 1 in 9460

Chapter 17 Solutions

BIOCHEMISTRY (LL)

Ch. 17 - RECALL Which reaction or reactions that we have...Ch. 17 - RECALL Which reaction or reactions that we have...Ch. 17 - RECALL What are the possible metabolic fates of...Ch. 17 - RECALL Explain the origin of the name of the...Ch. 17 - RECALL Define isozymes and give an example from...Ch. 17 - RECALL Why would enzymes be found as isozymes?Ch. 17 - RECALL Why is the formation of...Ch. 17 - REFLECT AND APPLLY Show that the reaction...Ch. 17 - REFLECT AND APPLLY What is the metabolic advantage...Ch. 17 - REFLECT AND APPLLY What are the metabolic effects...

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