slect all that apply Select the properties that apply to the secondary structure alpha helices (select all that apply).O can be Antiparallelcan be Parallelare typically right handedare typically left handedobeys n+4 ruleO are formed by the pattern of hydrogen bonding the backbone makes with itselfO are formed by the pattern of covalent bonds the backbone makes with itselfO are formed by the pattern of electrostatic attractions the backbone makes with itself

The alpha helix has a net dipole moment due to the arrangement of the backbone. This seems to…

Select the properties that apply to the secondary structure alpha helices (select all that apply). can be Antiparallel can be Parallel O are typically right handed O are typically left handed O obeys n+4 rule O are formed by the pattern of hydrogen bonding the backbone makes with itself O are formed by the pattern of covalent bonds the backbone makes with itself are formed by the pattern of electrostatic attractions the backbone makes with itself

Select the properties that apply to the secondary structure alpha helices (select all that apply). can be Antiparallel can be Parallel O are typically right handed O are typically left handed O obeys n+4 rule O are formed by the pattern of hydrogen bonding the backbone makes with itself O are formed by the pattern of covalent bonds the backbone makes with itself are formed by the pattern of electrostatic attractions the backbone makes with itself

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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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.
The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices unwind. c. sheet structures unfold. d. tertiary structure is changed. e. quaternary structures disassemble.
Explain what happens if even one amino acid is substituted for another in a polypeptide chain. Provide a specific example.
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
Tertiary structure of protein is maintained by Select one: a. Hydrogen bond b. All of these c. Di-sulphide bond d. Peptide bond
Both alpha-helices and beta-sheets (select any/all answers that apply): A. are examples of secondary structure. B. are stabilized by hydrogen-bonds between backbone atoms. C. are examples of tertiary structures. D. never contain proline residues. E. are commonly found in proteins.
Which of the following statements are correct about the native state of a protein (select all that apply)? A. Polar sidechains commonly interact with water B. Hydrophobic amino acids tend to be on surface of protein C. The sidechains of polar amino acids are most commonly found in the central core of a protein D. Formation of an alpha-helix is primarily driven by hydrogen bonds between the protein main chain, not sidechains. E. Secondary structure is largely driven by hydrophobic interactions
Carbon’s versatile bonding behavior allows it to form a variety of structures and are the base of all macromolecules. The diagram shows the structure of an amino acid, which is the monomer unit for proteins. Identify and describe the polymer structures of a protein that constitutes its unique conformation.
The tertiary structure of a protein is maintained by interactions between the side chains of amino acid residues one such interaction is between cysteine residues, sketch a covalent bond link that can form between side chains of two cysteine residues. Only relevant atoms that can form the link need to be shown
Draw the structure of 2 five-mers (draw backbones with side chains shown as R groups) forming a beta sheetwith two anti-parallel beta strands. Indicate the hydrogen bonds present inthissecondary 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
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