Please answer fast and all question. Which of the following types of bonds or interactions are least likely to beinvolved in formation and stabilization of the tertiary conformation of mostproteins?O ionicO peptideO disulfideO hydrogenCH,OHOHCH₂OHOHOHOHWhat type of macromolecule is this?O saccharideO nucleic acidO fatproteinWhich of the following is true?O B-DNA has both a minor and a major grooveO amino acids have different carboxylic acid groupsO the phosphate group is different between DNA and RNAOB-DNA is rare and has a long and slender shape

Tertiary structure of proteins can be defined as a three dimensional structure acquired by the…

Which of the following types of bonds or interactions are least likely to be involved in formation and stabilization of the tertiary conformation of most proteins? O ionic O peptide O disulfide O hydrogen CH, OH OH CH,OH OH R OH OH What type of macromolecule is this? O saccharide O nucleic acid O fat O protein

Which of the following types of bonds or interactions are least likely to be involved in formation and stabilization of the tertiary conformation of most proteins? O ionic O peptide O disulfide O hydrogen CH, OH OH CH,OH OH R OH OH What type of macromolecule is this? O saccharide O nucleic acid O fat O protein

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter3: The Chemistry Of Life: Organic Compounds

Section: Chapter Questions

Problem 9TYU: Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary...

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Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternary
Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.
Which of the following statement about proteins is correct a. alpha helix and Beta pleated sheets are considered quaternary structures b. a single polypeptide only has primary sytructure, secondary, tertiary, and quaternary structures require more than one polypeptide c. there are 30 essential amino acids that are the monomer building blocks of proteins d. polypeptides have a distinct polarity (directionality) with one end refered to as the free amino end, and the other called the free carboxyl end
Which of the following characterize -helix regions of proteins? (A) They all have the same primary structure. (8) They are formed principally by hydrogen bonds between a carbonyl oxygen atom in one peptide bond and the amide hydrogen from a different peptide bond. (C) They are formed principally by hydrogen bonds between a carbonyl atom in one peptide bond and the hydrogen atoms on the side chain of another amino acid. (D) They are formed by hydrogen bonding between two adjacent amino acids in the primary sequence. (€) They require a high content of proline and glycine
Which of the following characterize -helix regions of proteins? (A) They all have the same primary structure. (B) They are formed principally by hydrogen bonds between a carbonyl oxygen atom in one peptide bond and the amide hydrogen from a different peptide bond. (C) They are formed principally by hydrogen bonds between a carbonyl atom in one peptide bond and the hydrogen atoms on the side chain of another amino acid. (D) They are formed by hydrogen bonding between two adjacent amino acids in the primary sequence. (E) They require a high content of proline and glycine
In the peptide Ala – Gly – Val – Phe – Tyr, a carboxylate (-COO-) group would bound in which amino acid? A) Gly b) Ala c) Phe d) Tyr Which amino acid forms disulfide bonds? A) Met b) Cys c) Arg d) Pro The sequence Gly-Pro-Pro is often found in collagen. This would be a description of: a) primary structure b) secondary structure c) tertiary structure d) quaternary structure
Which of the following is NOT TRUE about secondary structure in proteins? (More than one may apply) A. Stabilized by non-covalent bonds B. Is illustrated by DnaA molecules interacting in the ori C. Unravels at high temperatures when intramolecular non-covalent bonds are destroyed D. Occurs in a subregion of a protein E. Exemplified by beta sheets F. Describes the order of amino acids in a polypeptide
1.Leucine is shown below. Suppose this amino acid was used to form the protein sequence Arg-Phe-Leu-Met-Pro. Select any atom that will be part of the protein backbone 2.This cartoon pf the protein hormone insulin illustrates what spaces of insulins structure? primary structure secondary structure tertiary structure quaternary structure
Which of the following statement is not true? In a secondary structure the consecutive residues have phi and psi values that are quite different. The Ramachandran diagram defines the restrictions of polypeptide backbone conformation. Two α helices with hydrophobic side chains repeated in a regular pattern can form dimeric structures in water. Greek key motifs occur frequently in antiparallel β structures. Both α helices and β sheets can be amphipathic.
Which of the following is NOT an example of protein secondary structure? a. alpha-helix b. beta sheets c. beta turn d. coiled coil e. loops
Which of the following statements about alpha-helix and beta-sheet structure are true? More than one answer is correct. -they are aspects of protein secondary structure. -they are maintained by hydrogen-bonding interactions within the polypeptide backbone. -most proteins fall into one of two categories: those composed entirely of alpha-helix, and those composed entirely of beta-sheet. -in both alpha-helix and beta-sheet, each amino acid (at position n) interacts with another amino acid at position n+4. -alpha-helix contains only hydrophobic amino acids, while beta-sheet contains only hydrophilic amino acids. More than one answer is correct I am confused
Which of the following is/are least likely to be found in an alpha helix because it has an inappropriate Phi angle. a Polar charged amino acids b Proline c Nonpolar amino acids d Glycine e Polar uncharged amino acids