Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Textbook Question
Chapter 4, Problem 6RE
REFLECT 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.
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Biochemistry
Ch. 4 - RECALL Match the following statements about...Ch. 4 - RECALL Define denaturation in terms of the effects...Ch. 4 - RECALL What is the nature of random structure in...Ch. 4 - REFLECT AND APPLY Suggest an explanation for the...Ch. 4 - REFLECT AND APPLY Rationalize the following...Ch. 4 - REFLECT AND APPLY Glycine is a highly conserved...Ch. 4 - REFLECT AND APPLY A mutation that changes an...Ch. 4 - REFLECT AND APPLY A biochemistry student...Ch. 4 - RECALL List three major differences between...Ch. 4 - RECALL What are Ramachandran angles?
Ch. 4 - Prob. 11RECh. 4 - Prob. 12RECh. 4 - RECALL List some of the differences between the...Ch. 4 - RECALL List some of the possible combinations of...Ch. 4 - RECALL Why is proline frequently encountered at...Ch. 4 - RECALL Why must glycine be found at regular...Ch. 4 - REFLECT AND APPLY You hear the comment that the...Ch. 4 - REFLECT AND APPLY Woolen clothing shrinks when...Ch. 4 - RECALL Draw two hydrogen bonds, one that is part...Ch. 4 - RECALL Draw a possible electrostatic interaction...Ch. 4 - RECALL Draw a disulfide bridge between two...Ch. 4 - RECALL Draw a region of a polypeptide chain...Ch. 4 - REFLECT AND APPLY The terms configuration and...Ch. 4 - REFLECT AND APPLY Theoretically, a protein could...Ch. 4 - REFLECT AND APPLY What is the highest level of...Ch. 4 - RECALL List two similarities and two differences...Ch. 4 - RECALL What are the two critical amino acids near...Ch. 4 - RECALL What is the highest level of organization...Ch. 4 - RECALL Suggest a way in which the difference...Ch. 4 - RECALL Describe the Bohr effect.Ch. 4 - RECALL Describe the effect of 2,...Ch. 4 - RECALL How does the oxygen-binding curve of fetal...Ch. 4 - RECALL What is the critical amino acid difference...Ch. 4 - REFLECT AND APPLY In oxygenated hemoglobin,...Ch. 4 - REFLECT AND APPLY You are studying with a friend...Ch. 4 - REFLECT AND APPLY How does the difference between...Ch. 4 - REFLECT AND APPLY Suggest a reason for the...Ch. 4 - Prob. 38RECh. 4 - REFLECT AND APPLY Why is fetal Hb essential for...Ch. 4 - BIOCHEMICAL CONNECTIONS Why might you expect to...Ch. 4 - REFLECT AND APPLY When deoxyhemoglobin was first...Ch. 4 - BIOCHEMICAL CONNECTIONS What is the direct cause...Ch. 4 - BIOCHEMICAL CONNECTIONS What is the effect of the...Ch. 4 - BIOCHEMICAL CONNECTIONS Why do scientists believe...Ch. 4 - Prob. 45RECh. 4 - BIOCHEMICAL CONNECTIONS What is BCL11A and how is...Ch. 4 - BIOCHEMICAL CONNECTIONS Given the purpose of...Ch. 4 - Prob. 48RECh. 4 - REFLECT AND APPLY Comment on the energetics of...Ch. 4 - RECALL What is a chaperone?Ch. 4 - Prob. 52RECh. 4 - Prob. 53RECh. 4 - Prob. 54RECh. 4 - RECALL What are some diseases caused by misfolded...Ch. 4 - RECALL What causes protein aggregates to form?Ch. 4 - Prob. 57RECh. 4 - Prob. 58RECh. 4 - BIOCHEMICAL CONNECTIONS What aspects of the...Ch. 4 - Prob. 60RECh. 4 - Prob. 61RE
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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 Comment on the energetics of protein folding in light of the information in this chapter.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 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 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 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 A friend tells you that only four different kinds of bases are found in RNA. What would you say in reply?arrow_forwardREFLECT AND APPLY Would you expect tRNA or mRNA to be more extensively hydrogen bonded? Why?arrow_forward
- REFLECT 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_forwardREFLECT AND APPLY Common proteins are polymers of 20 different amino acids. How big a protein (how many amino acid residues) would be necessary to have an Avogadros number of possible sequences?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
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