Consider the sequences (i-iv) that represent sections of a protein.) -АЕEAAAAMAАAАMAAYii) -KVIVVVTVVTVVVKVV-iii) -GPPGPPGPPGPPGPPGPP-iv) -WYFWYFWYFVVFFFVV-Which of the following statements is likely to be true?O Sequence (iv) is likely to have an alpha-helix structure.O Sequence (i) is likely to have an alpha-helix structure and sequences (i) and (iv) are most likely to have beta-sheet structuresO Sequence (ii) is ikely to be a metal-binding domain.O Sequence (i) is likely to have a beta-sheet structure and sequences (ii) and (iv) are most likely to have alpha-helix structuresO Sequence (ii) is most likely have a beta sheet structure with a hairpin turn.

Secondary structure is the formation of regular patterns through interaction between nearby…

Consider the sequences (i-iv) that represent sections of a protein. i) -AEEAAAAMAAAAMAAY ii) -KVIVVVTVVTVVVKVV- iii) -GPPGPPGPPGPPGPPGPP- iv) -WYFWYFWYEVVEFEVV- Which of the following statements is likely to be true? Sequence (iv) is likely to have an alpha-helix structure. Sequence (i) is likely to have an alpha-helix structure and sequences (ii) and (iv) are most likely to have beta-

Consider the sequences (i-iv) that represent sections of a protein. i) -AEEAAAAMAAAAMAAY ii) -KVIVVVTVVTVVVKVV- iii) -GPPGPPGPPGPPGPPGPP- iv) -WYFWYFWYEVVEFEVV- Which of the following statements is likely to be true? Sequence (iv) is likely to have an alpha-helix structure. Sequence (i) is likely to have an alpha-helix structure and sequences (ii) and (iv) are most likely to have beta-

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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You will now build a 15 amino acid peptide using another paper or wire backbone as you did above. You will pick 15 amino acids, matching the criteria below, and put them onto your backbone about 3 inches apart. This will be the primary structure of your novel protein. Select 15 amino acids that meet the following criteria 6 hydrophobic R groups 2 acidic R groups 2 basic R groups 2 cysteine R groups 3 hydrophilic R groups Place the R groups in any order you choose on your paper or wire backbone as you did above. Start at the N-terminus and place each R group about 3 inches apart until all 15 are attached to the mini toolbar. You have just built the primary structure of your protein. Question 1: Record the sequence of amino acids in your protein, starting with the N-terminus. The N-terminus is the end of the polypeptide that has a free nitrogen group. The C-terminus, or carboxyl end, will have a free carboxyl group. You can use the three letter amino acid abbreviation to…
Which of the following statements are False? (i) Parallel b-sheets characteristically distribute hydrophobic side chains on both sides of the sheet, and antiparallel B-sheets are usually arranged with all their hydrophobic residues on one side of the sheet. (ii) Planarity of the peptide bond means that no rotation occurs about the N-Ca bond while rotation is allowed about the C(O)-N and Ca-C(O) bonds. (iii) Silk fibers consist of fibroin proteins consisting of alternating A and G or S residues. (iv) If an aspartic acid residue were present in the interior of a globular protein, it would most likely be deprotonated and thus negatively charged.
Answer the following using the structure: a. Is this a purine or pyrimidine? b. Is this a deoxyribonucleotide or a ribonucleotide? c. Indicate the component that changes this from a nucleoside to a nucleotide.
A. Where would you expect valine, leucine, and isoleucine to be located in a polypeptide? (Inside or outside)? Explain your answer using the properties of the amino acids listed. B.How would your answer change, if the amino acids were Lysine and Histidine?
Can you please solve this question for me?
Assume you were given a mixture consisting of one molecule each of all possible sequences of a smallish protein of molecular weight 4800 daltons. If the average molecular weight of an amino acid is, say, 120 daltons, how much would the sample weigh? How big a container would you need to hold it?
Which of the following is true A) The disulfide bridges formed by reduction of the sulfhydryl groups on cysteine destabilizes protein tertiary structure. B) The disulfide bridges formed by oxidation of the sulfhydryl groups on cysteine destabilizes protein tertiary structure. C) The disulfide bridges formed by oxidation of the sulfhydryl groups on cysteine stabilizes protein tertiary structure. D) The disulfide bridges formed by reduction of the sulfhydryl groups on cysteine stabilizes protein tertiary structure.
Select the term in column B which best matches the description in column A. There are more terms then needed. Column A Column B 1. The pentose sugar found in DNA. a) Cis fatty acid b) Trans fatty acid c) Coenzyme d) Cofacipr 2. Commonly referred to as "insoluble fiber". 3. Considered to be an amphipathic molecule. 4. A molecule with the formula C18H3602 is probably a e) Phospholipid 5. Bond created during the formation of the primary structure of a protein. ) Glycogen 6. A non-protein organic molecule needed for proper enzyme functioning. g) Cellulose 7. Pyrimidine base found only in RNA. h) Galactose i) Fructose 8. Increasing the number of these molecules in the cell membrane would increase the permeability of the cell membrane. i) Thymine k) Uracil 9. Bond which connects nucleotide monomers together. 1) Fatty acid m) Disaccharide n) Peptide bond o) A-Helix p) B-Pleated Sheet q) Ribose r) Deoxyribose 10.
One technique that is used when attempting to solve the crystal structure of a large protein is not to solve the structure of the whole protein itself. Instead, the protein is broken down into smaller components and the structure of the smaller components is what is solved. Of course, when performing this technique, it must be ensured that the process of breaking down the protein into smaller components does not drastically change the structure of the smaller components. With this in mind, where would be the best locations to cut a protein? At the beginning and end of secondary structures. At beginning and end of protein domains. O At the beginning and end of motifs. At the beginning and end of protein subunits.
A researcher isolates a new protein and finds that it contains 0.755% serine by weight upon amino acid analysis. The molecular mass of serine is 105 g.mol-¹. What is the minimum molecular mass for the protein assuming only one Ser residue per protein molecule? mmin = The researcher estimates the molecular mass of the protein using gel electrophoresis. From this estimated molecular mass, the researcher concludes the protein contains 3 Ser residues. What is the estimated molecular mass of the protein as shown by gel electrophoresis? g.mol-¹ mest = g.mol-1
A spheroidal bacterium with a diameter of 1.0 μm (micrometer, 1 μm = 10-6) contains 25,000 molecules of the protein hexokinase. What is the molar concentration of the protein inside the cell?