Shown below is a section of beta-sheet from the protein thioredoxin. Amide nitrogens are indicated by circled Ns, carbonyl oxygens by Os, and hydrogen bonds by gray lines. JO (N MO MO (N) amm strand 1 [Select] strand 2 [Select ] O 1 2 3 4 For each strand of the sheet (1, 2, 3, 4) indicate the direction (top or bottom) of the N-terminus. strand 3 [Select] strand 4 [Select] Nam strands 2 and 3 Determine the orientation (parallel or antiparallel) of each adjacent strand to one another. strands 1 and 2 [Select] O(N) [Select] strands 3 and 4 [Select]

Shown below is a section of beta-sheet from the protein thioredoxin. Amide nitrogens are indicated by circled Ns, carbonyl oxygens by Os, and hydrogen bonds by gray lines. JO (N MO MO (N) amm strand 1 [Select] strand 2 [Select ] O 1 2 3 4 For each strand of the sheet (1, 2, 3, 4) indicate the direction (top or bottom) of the N-terminus. strand 3 [Select] strand 4 [Select] Nam strands 2 and 3 Determine the orientation (parallel or antiparallel) of each adjacent strand to one another. strands 1 and 2 [Select] O(N) [Select] strands 3 and 4 [Select]

Introduction to General, Organic and Biochemistry

11th Edition

ISBN:9781285869759

Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Chapter23: Enzymes

Section: Chapter Questions

Problem 23.15P: 5 At a very low concentration of a certain substrate, we find that when the substrate concentration...

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Similar questions

22-35 Why is histidine considered a basic amino acid when the pKa of its side chain is 6.0?
For the tripeptide SerValMet a. What amino acid is located at the peptides N-terminal end? b. What amino acid is located at the peptides C-terminal end? c. How many peptide bonds are present? d. How many amide linkages are present?
5 Which of the following is a correct statement describing the induced-fit model of enzyme action? Substrates fit into the active site: (a) because both are exactly the same size and shape. (b) by changing their size and shape to match those of the active site. (c) by changing the size and shape of the active site upon binding.
22-82 (Chemical Connections 22H) How does the fiberscope help to heal bleeding ulcers?
How many of the -amino acids shown in Table 26-1 contain aromatic rings? How many contain sulfur? How many contain alcohols? How many contain hydrocarbon side chains?
7 Enzymes are long protein chains, usually containing more than loo amino acid residues. Yet the active site contains only a few amino acids. Explain why the other amino acids of the chain are present and what would happen to the enzyme activity if the enzyme’s structure were changed significantly.
5 At a very low concentration of a certain substrate, we find that when the substrate concentration doubles, the rate of the enzyme-catalyzed reaction also doubles. Would you expect the same finding at a very high substrate concentration? Explain.
22-24 Draw the most predominant form of histidine at its isoelectric point.
0 Explain the relationship between transition-state analogs and abzymes.
22-91 Which amino acid does not rotate the plane of polarized light?
22-71 Which amino acid side chain is most frequently involved in denaturation by reduction?
22-59 What is the effect of salt bridges on the tertiary structure of proteins?