Answered: Which of the following is incorrect?… | bartleby

Nutrition Now

8th Edition

ISBN:9781337415408

Author:Brown

Publisher:Brown

Chapter15: Proteins And Amino Acids

Section: Chapter Questions

Problem 12RQ

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Question

Which of the following is incorrect?
a. None; all the other choices are correct
Ob.
Disulfide bonds can be formed between two Cys
W is the least abundant amino acid in proteins
Od. Leu is the most abundant amino acid in proteins
C.

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A C2 G This a photograph of an actual polyacrylamide gel that has been run with samples of protein. For each question, write the letter from the item in the gel that best matches the word or concept that is described. Answers may be used once, more than once, or not at all. There may be more than one correct answer per question. 1. Band 2. Lane 3. Well 4. Will protein migrate through the gel from A to B or will it migrate from B to A? 5. Which end is nearest the negative electrode, A or B? 6. Which contains smaller protein fragments, F or G? 7. Which letter indicates the highest concentration of protein fragments that are the same size 8. Where would a sample of protein be loaded? B.
+H₂N-CH-COO™ T CH₂ I CH₂ 1 CH₂ I +H₂N-CH₂ A. O amino acid C amino acid D O amino acid E amino acid B +H₂N-CH-COO™ I CH₂ I CH₂ 1 O amino acid A C=0 B. If the pH decreases enough, this amino acid will become protonated and could contribute to the denaturation of the protein. +H₂N-CH-COO™ 1 CH₂ I OH C. +H₂N-CH-COO™ CH H₂C CH3 D.
A. What type of bond is ( the two mark wtih questions mark) B. What special amino acid side chain is involved in forming these bond C. Does this bond form unde reduction or oxidizing D. Is this bond seen more in cytoplsmic proteins or in extravellular protein
+H₂N-CH-COO™ 1 CH₂ I CH₂ 1 CH₂ I +H₂N-CH₂ A. O amino acid B amino acid D amino acid A amino acid E +H₂N-CH-COO™ 1 CH₂ T O amino acid C CH₂ 1 C=0 B. This amino acid participates in hydrophobic interactions to stabilize protein conformation. +H₂N-CH-COO™ I CH₂ I OH C. +H₂N-CH-COO™ I CH H₂C CH3 D.
Which of the following describes the most likely outcome of a mutation that causes a sin- gle amino acid to be removed from a protein subunit? A It will affect the primary, secondary, and tertiary structures of the protein. B с D It will affect the secondary and tertiary structures of the protein but not the primary structure. There will be no observable effect on the structure of the protein. It will change the primary structure of the protein without affecting other structures in the protein.
Chicken egg contains a lot of proteins which supports the growth and development of the chicken embryo. The chicken egg was placed on high heat (100°C) until it forms a solid structure. Which of the following statements is correct about the given scenario? O The increase in temperature may interfere intermolecular forces of attraction that stabilizes the native conformation. O Structural and functional characteristics of proteins remain intact even temperature was increased to boiling O Extreme temperature conditions may result to irreversible denaturation due to destruction of primary. secondary, tertiary, and quaternary structures By decreasing the temperature, the egg embryo can still develop, and grow to become a chicken because renaturation may take place.
positive (basic), or polar negative (acidic) folded protein in the aqueous cellular environment, is which is responsible for major structural features of the major property of the amino acid side chains, their a.tertiary amine length b.presence of carbons c.heptacyclic fold strength d.formation of glycosides e.bydrophobic vs hydrophilic character AQuestion 27 noa g to c amino acids can be polar neutral, polar positive (basic), or polar negative (aciale) a.sterol ah orgo s a b.glycolic c.non-polar Hydrophilic e.hydrophobic
A protein has a mutation of a glycine to a lysine. Which best predicts the impact of this mutation on the overall protein structure and function? H.N, *NH3 Glycine Lysine O A small hydrophobic amino acid has been replaced with a large hydrophilic amino acid, and this may change folding O A small hydrophilic amino acid has been replaced with a large hydrophobic amino acid, and this may change folding O These residues are similar in chemical properties, and there will be little impact on folding O This mutation may disrupt hydrogen bonds, which would disrupt the tertiary structure
Which of these amino acids is a polar, uncharged amino acid? (Select all that apply, if necessary.) A. B. D. E. CHLO H₂N-CH-C CH₂ CH₂ CH₂ NH C=NH2 NH₂ amino acid A amino acid C amino acid D amino acid B amino acid E H₂N-CH-C CH₂ _i_g C. H₂N-CH-C- CH2₂ I CH₂ =0 NH₂ H₂N-CH- CH₂ CH-CH3 CH3 H₂ND H₂N-CH- | CH₂ Ï OH
Which of the following most directly applies to the formation of the secondary structures of proteins? A B с D formation of ionic bonds between the R groups of two polypeptides formation of nonpolar interactions between two R groups on the same polypeptide formation of covalent bonds via dehydration reactions between two amino acids formation of hydrogen bonds between between amino and carboxyl groups
Which of the following statements about protein structure is CORRECT O a. Fibrous proteins can have rigid quaternary structure O b. The stability of the quaternary structure in proteins is mainly a result of covalent bonds among the subunits O c. The denaturation of proteins always leads to irreversible loss of secondary and tertiary structure d. The information required for the correct folding of a protein is contained in the specific sequence of amino acids along the polypeptide chain O e. The formation of a disulfide bond in a protein requires that the two participating cysteine residues be adjacent to each other in the primary sequence of the protein
Refer to the figure below, what are the following forces of attraction is involved in the protein folding for each number. 1. 2. CH₂ C-OH CH₂ 3. 4. CH H₂C CHS H₂C CH3 CH CH₂-S S-CH₂ 3 –CH,CH,CH, CH, NH

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