What is the general characteristic of protein domains?A. All protein domains exhibit both a and B structuresB. Protein domains constitute supersecondary structuresthat have specific biological functions in proteins.C. Most protein domains can be hydrolyzed from parentpolypeptide chains while retaining functions and/orstructures that are conserved.D. Protein domains constitute the structural block fromwhich the protein is builtE. Protein domains contain motifs that are the binding sitesfor prosthetic groups such as heme, or the iron-sulfurclusters.

Proteins are linear heteropolymers of twenty standard amino acids attached through the peptide…

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Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Describe the covalent structure of an amino acid. Then describe the 4 levels of protein folding. After a protein is folded, what are 2 post-translational modifications that can take place to impact protein function.
At what level of protein structure does each of the following denaturation act? a. heat b. strong acid c. saturated salt solution d. organic solvents (e.g., alcohol or chloroform)
Many proteins contain one or more motifs built from particular combinations of secondary structure. Describe the three common structural motifs and describe some of the general functions of protein domains on the extracellular membrane surface, within the membrane, or on the cytosolic face of the membrane. Whatr are the biological activities of proteins are affected by chemical modifications.
What is one of the determining factors in the three-dimensional structure of a protein? A.The location of alpha sheets and beta propellersB.The presence of another proteinC.The location of hydrophobic and hydrophilic amino acidsD.The presence of nucleic acids such as DNA
Describe the two types of secondary structure apolypeptide can attain. Which proteins can achievequaternary structure? Which protein structure(s) are alteredby denaturation?
Which of the following statements are correct about protein structure (select all that apply)? A. Post-translational modifications such as glycosylation or phosphorylation may alter the structure of a protein B. Only amino acids with a net charge may interact with other amino acids C. The 3D structure of a protein is determined primarily by the protein backbone/main chain conformation while the amino acid sidechains play only a minor role. D. Hydrophobic interactions play a key role in protein folding E. Amino acid sidechains contribute to 3D structure through their ability to form hydrogen bonds with other amino acids
Denaturation is the loss of protein function from structuralchange or chemical reaction. At what level of proteinstructure or through what chemical reaction does each ofthe following denaturation agents act?a. heatb. strong acidc. saturated salt solutiond. organic solvents (e.g., alcohol or chloroform)
A protein in its native three dimensional conformation is cleaved with trypsin. According to the amino acid sequence, there are 9 residues where trypsin could cleave, yet only 3 fragments were produced from the digest. What conclusion can be made about protein structure that would lead to this result? The protein has multiple domains b. The protein is highly compacted, minimally accessible by solvent molecules c. The protein has quaternary structure d. The protein has a dynamic structure, highly accessible by solvent molecules e. The protein is compromised only of alpha helices
Understand that some amino acids are nonpolar, polar/uncharged, charged. Explain how this is related to the 4 levels of protein structure.
why do transmembrane proteins cross the phospholipid bilayer as an a-helix or B-barrel? A. These structures arrange polar peptide bonds and hydrogen bonds to the exterior of the helix or barrel while nonpolar side chains are on the interior. B. These structures sequester polar peptide bonds and hydrogen bonds to the interior of the helix or barrel while nonpolar sidechains are on the exterior.
Which of the following events would have the strongest influence on the overall three-dimensional structure of a protein? Select one: a. Valines angle away from surrounding water molecules as the protein folds b. Two polypeptide strands, running in opposite directions, form hydrogen bonds with each other Oc. Another protein sticks to its outside d. The amine and carboxylic ends of the protein chain are left unreacted Oe. Three glycines are chained together Clear my choice Previous page esc ! 1 ← 2 3 W 3 E 38 $ 4 R 5 T 80 MacBook Pro A 6 Y & 7 U 8 I 9 4 1 O 0 P TO + ( W Next pa
Indicate the level(s) of protein structure to which each of thefollowing contributes:a. amino acid sequenceb. b-pleated sheetc. hydrogen bondd. disulfide bond

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What is the general characteristic of protein domains? A. All protein domains exhibit both a and B structures B. Protein domains constitute supersecondary structures that have specific biological functions in proteins.