Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Chapter 3, Problem 5RE
RECALL Identify the nonpolar amino acids and the acidic amino acids in the following peptide:
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Biochemistry
Ch. 3 - RECALL How do D-amino acids differ from L-amino...Ch. 3 - RECALL Which amino acid is technically not an...Ch. 3 - RECALL For each of the following, name an amino...Ch. 3 - RECALL Identify the polar amino acids, the...Ch. 3 - RECALL Identify the nonpolar amino acids and the...Ch. 3 - RECALL Are amino acids other than the usual 20...Ch. 3 - MATHEMATICAL Predict the predominant ionized forms...Ch. 3 - MATHEMATICAL Draw structures of the following...Ch. 3 - MATHEMATICAL Predict the predominant forms of the...Ch. 3 - MATHEMATICAL Calculate the isoelectric point of...
Ch. 3 - MATHEMATICAL Sketch a titration curve for the...Ch. 3 - MATHEMATICAL Sketch a titration curve for the...Ch. 3 - MATHEMATICAL An organic chemist is generally happy...Ch. 3 - MATHEMATICAL Sketch a titration curve for aspartic...Ch. 3 - REFECT AND APPLY Suggest a reason why amino acids...Ch. 3 - REFECT AND APPLY Write equations to show the ionic...Ch. 3 - REFECT AND APPLY Based on the information in Table...Ch. 3 - REFECT AND APPLY If you were to have a mythical...Ch. 3 - REFECT AND APPLY What would be the pI for the...Ch. 3 - REFECT AND APPLY Identify the charged groups in...Ch. 3 - REFECT AND APPLY Consider the following peptides:...Ch. 3 - REFECT AND APPLY In each of the following two...Ch. 3 - REFECT AND APPLY Could the amino acid glycine...Ch. 3 - RECALL Sketch resonance structures for the peptide...Ch. 3 - RECALL How do the resonance structures of the...Ch. 3 - REFECT AND APPLY Would the peptide group be planar...Ch. 3 - Prob. 27RECh. 3 - REFECT AND APPLY Consider the peptides...Ch. 3 - REFECT AND APPLY Would you expect the titration...Ch. 3 - REFECT AND APPLY What are the sequences of all the...Ch. 3 - REFECT AND APPLY Answer Question 30 using...Ch. 3 - REFECT AND APPLY Most proteins contain more than...Ch. 3 - REFECT AND APPLY If the amino acids alanine and...Ch. 3 - Prob. 34RECh. 3 - REFECT AND APPLY Would the presence of a chiral...Ch. 3 - REFECT AND APPLY What might you infer (or know)...Ch. 3 - Prob. 37RECh. 3 - REFECT AND APPLY Suggest a reason why the amino...Ch. 3 - REFECT AND APPLY Consider the peptides...Ch. 3 - Prob. 40RECh. 3 - Prob. 41RECh. 3 - REFECT AND APPLY You are studying with a friend...Ch. 3 - Prob. 43RECh. 3 - REFECT AND APPLY Suggest a reason (or reasons) why...Ch. 3 - Prob. 45RECh. 3 - REFECT AND APPLY Speculate on the properties of...Ch. 3 - RECALL What are the structural differences between...Ch. 3 - RECALL How do the peptide hormones oxytocin and...Ch. 3 - RECALL What is the role of the disulfide bond in...Ch. 3 - RECALL Is it possible to form cyclic peptides...Ch. 3 - Prob. 51RECh. 3 - RECALL What types of experiments led to evidence...Ch. 3 - Prob. 53RECh. 3 - THOUGHT QUESTION Imagine we identify a gene that...
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- REFLECT 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_forwardRECALL What is qPCR?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
- REFLECT 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 Comment on the energetics of protein folding in light of the information in this chapter.arrow_forwardREFLECT AND APPLY Glycine is a highly conserved amino acid residue in proteins (i.e., it is found in the same position in the primary structure of related proteins). Suggest a reason why this might occur.arrow_forward
- REFLECT AND APPLY Is amino acid activation energetically favored? Why or why not?arrow_forwardRECALL Is it possible to form cyclic peptides without bonds between side chains of the component amino acids?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_forward
- 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 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 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
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