Which of the following best describes where the amino acids isoleucine and tryptophan aremost likely to be found in the tertiary structure of a protein?HNH₂NOHIleоH₂NOHTrpin the hydrophilic interior of the protein due to their ability to form side chain hydrogen bonds witheach otherin the interior of the folded protein away from water, due to their hydrophobic natureon the exterior surface of the folded protein where contact with water is greatest, due to theirhydrophilic natureat the N-terminal end of the protein

1. The property of hydrophobicityTryptophan and isoleucine are hydrophobic amino acids. Because of…

Answered: Which of the following best describes…

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

See similar textbooks

Similar questions

Researchers discover a new amino acid. Its R-group exclusively has hydrogen and carbon atoms. What behavior will this amino acid show? O Relative to the amino acids found in organisms, its interactions with water will be very high. It is hydrophilic. Relative to the amino acids found in organisms, its interactions with water will be intermediate. It is hydrophobic.
The amino acid histidine has ionizable groups with pK, values of 1.8, 6.0, and 9.2, as shown. COOH H₂N-CH CH, H pH = 1.29 COO H₂N-CH 1.8 CH pk, lonizable -COOH-COO- group Incorrect CH, H COO H₂N-CH 6.0 CH pk, CH, H H N CH -HisH¹-His COO H₂N-CH NH - NH, A biochemist makes up 85 mL of a 0.10 M solution of histidine at a pH of 5.5. She then adds 60 mL of 0.10 M HCI. What is the pH of the resulting solution? CH, H 9.2 C pk CH Macmillan Iraming T im be the [His IM.
1. Determine whether each of the following statements describes the primary, secondary, tertiary, or quaternary stucture of a protein. а. Peptide bonds join amino acids in a polypeptide chain. b. Two polypeptide chains are held together by hydrogen bonds. С. Hydrogen bonds form between adjacent segments of the backbone of the same protein to form a "folded fan" structure. 2. List the type of denaturing agent described by the following treatments: a. disrupting the disulfide bonds in hair to straighten it b. baking the proteins in dough to make bread
Which statement is NOT true about a peptide bond? O The peptide bond is longer than the typical carbon-nitrogen bond. CO The carbonyl oxygen and the amide hydrogen are most often in a frans configuration with respect to another. O Rotation is restricted about the peptide bond. The peptide bond has partial double-bond character.
Which amino acids have R groups with an additional chiral carbon? - Cysteine - Isoleucine - Threonine -Histidine - Tryptophan - Tyrosine - Methionine
a protein chain. D) removing helping molecules such as heme. E) breaking disulfide bridges. 10) When this tripeptide undergoes acid hydrolysis, what are the amino acids formed? Draw the structures. CH3 O Cys H₂O H₂N-CH-CN-CH₂-C-N-CH-C-0 -CH,−0 Ser Is this bonding polar or non-polar? CH₂S—S-CH₂- CH₂O Phe Cys H Alanylglycylserine (Ala-Gly-Ser, AGS) What type of bonding holds the amino acid R group together? HO CH3 CH₂ H₂O OH NH₂ O Asn 11. What kind of interaction would form between these R groups of an amino acid. Leu Hydrolysis C-CH₂- CH-CH₂- CH₂ O CH₂- 12. What is a peptide bond? How are peptide bond form? Give an example. 13. Draw the structure of tyrosine? Is it a polar or nonpolar amino acid? Draw the major form of tyrosine, pl = 7.3, at a pH of 4 and 2) pH 10 Which structure will not be disrupted during acid hydrolysis a) Amino acid b) Primary structure b) Secondary structure What is a globular protein? True / d) quaternary structure aturation of a protein a.occurs when a change…
Which of the following is FALSE for protein folding/structure. O Intermolecular interactions occur faster than intramolecular interactions. The hydrophobic effect is present almost immediately. Hydrogen bond formation in the backbone begins almost immediately. Side chain interactions slightly lag behind the backbone interactions. All these answers are TRUE.
Which statement is false about a globular protein that performs its biological function as a single independent polypeptide chain? O a. Its tertiary structure is likely stabilized by the interactions of amino acid side chains in non-neighboring regions of the polypeptide chain. It likely has extensive quaternary structure to maintain its globular shape. b. Oc. Non-covalent forces are the primary source of stability for the secondary and tertiary structure. Ⓒd. it could contain a-helices that are stabilized by hydrogen bonding.
`The chemical properties can differ between amino acids due to what main factor? carboxylic acid group R group (side chain) molecular weight armine group
Would you expect these two tripeptides to have the same function in the body? Why or why not? His-Pro-Val VS Val-Pro-His A) Yes, these two tripeptides are identical. B) Yes, as long as two peptides have the same amino acids, no matter the sequence, they will have the same function. C) Yes, the body recognizes all tripeptides the same. D) No, structure determines function, and their structures are different. E) There is no way to determine this.
Question 8 of 15 Provide the correct three-letter abbreviation for the following amino acid: O || H₂N-CH-C-OH Met ठे CH₂ CH₂ C=O OH Ala Arg Asn. Asp Cys Glu Gln Gly His lle Leu Lys Phe Pro Ser Thr Trp Tyr Val
Part D Complete the sentences to explain the differences between tertiary and quaternary structures of proteins. Match the words in the left column to the appropriate blanks in the sentences on the right. Make certain each sentence is complete before submitting your answer. three-dimensional shape two or more peptide subunits oxygen and disulfide bonds -R groups two-dimensional shape two or more polypeptide chains disulfide bonds and salt bridges -C(O)NH groups Submit Request Answer The tertiary structure is determined by the interactions of describes the of the protein In the quaternary structure, Reset Help These interactions, such as interact to form an active protein.

SEE MORE QUESTIONS

Recommended textbooks for you

Chemistry

ISBN:

9781305957404

Author:

Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:

Cengage Learning

Chemistry

ISBN:

9781259911156

Author:

Raymond Chang Dr., Jason Overby Professor

Publisher:

McGraw-Hill Education

Principles of Instrumental Analysis

Chemistry

ISBN:

9781305577213

Author:

Douglas A. Skoog, F. James Holler, Stanley R. Crouch

Publisher:

Cengage Learning

Chemistry

ISBN:

9781305957404

Author:

Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:

Cengage Learning

Chemistry

ISBN:

9781259911156

Author:

Raymond Chang Dr., Jason Overby Professor

Publisher:

McGraw-Hill Education

Principles of Instrumental Analysis

Chemistry

ISBN:

9781305577213

Author:

Douglas A. Skoog, F. James Holler, Stanley R. Crouch

Publisher:

Cengage Learning

Organic Chemistry

Chemistry

ISBN:

9780078021558

Author:

Janice Gorzynski Smith Dr.

Publisher:

McGraw-Hill Education

Chemistry: Principles and Reactions

Chemistry

ISBN:

9781305079373

Author:

William L. Masterton, Cecile N. Hurley

Publisher:

Cengage Learning

Elementary Principles of Chemical Processes, Bind…

Chemistry

ISBN:

9781118431221

Author:

Richard M. Felder, Ronald W. Rousseau, Lisa G. Bullard

Publisher:

WILEY

SEE MORE TEXTBOOKS