Which of the following statements are true concerning the structure of proteins?I. The same intermolecular force is responsible for the arrangement of a-helices and B-pleated sheets.II. Disulfide links contribute to the tertiary structure of proteins not the quaternary structure.III. The order of the peptide bonds describes its primary structure.IV. The hydrophobic side chains generally point toward the outside of the protein in water.V. Only dispersion, dipole-dipole, ionic and hydrogen bonding are responsible for the quaternary structure of proteins.Select one:O I and IIO Ill onlyO IV and VO Il and III

When amino acids are linked together as peptide linkage and number of linked amino acids are in high…

Answered: Which of the following statements are…

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...

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09:56 7 < Question 18 of 19 The amino acid structure shown here is known as a(n) H₂N+ A) primary structure. B) secondary structure. C) C-terminus. D) N-terminus. Periodic Table Submit
1a. Describe the formation of a bond between two amino acids that craves a peptide. 1B. The image below is a dipeptide. How can you always identified the peptide bond between amino acids?
If a protein contains four different SH groups, how many different disulfide bonds are possible if only a single disulfide bond is formed? How many different disulfides are possible if two disulfide bonds are formed?
Which of the following statement about the conformation of protein is true? a. Denaturation of protein causes the changes in the primary structure of the protein b. Primary structure of protein refers to the sequence of amino acid linked by hydrogen bonds c. Alpha-helix and beta-sheet are two types of secondary structures found in proteins d. Amino acids are covalently linked by glycosidic bonds
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
The building blocks of all proteins are a. pleated sheetsb. alpha amino acidsc. alpha helicesd. tertiary structurese. none of these
Explain the polypeptide chain structure
What do your findings suggest about the stability of proteins in the presence of organic solvents?
6. The primary structure of a protein involves which of the following? a) Van der Waals forces b) peptide bonds c) hydrogen bonds d) disulfide bonds e) hydrophilic forces
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 interaction(s) is/are involved in the primary structure of a protein (choose all that apply)? a. hydrogen bonding b. salt bridge c. hydrophobic effects d. covalent peptide bond
Question 7 Select the correct option(s) regarding denaturation of proteins. O Proteins can be denatured by extremes in environmental conditions including Temp and pHt, as well as, upon exposure to high concentrations of oxidants and ure O Disruption of H-bonds can lead to a loss of secondary protein structure and thus denaturation O Following denaturation, some proteins can renature if native bonding can be re-established. O All options shown regarding denaturation of proteins are correct. When bonds that hold the 30 confirmation of an enzyme break, shape of the active site changes, which leads to inefficient binding of substrate molecules 1

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