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Concept explainers
(a)
Interpretation: The given statement whether applies to primary, secondary, tertiary protein structure or not has to be stated.
Concept introduction: The primary protein structure is the order of linking of the amino acids in proteins.
The arrangement of the portion of protein backbone in space gives the secondary protein structure.
The three-dimensional shape of the proteins obtained as a result of the interactions between the amino acid side chains is called the tertiary protein structure.
(b)
Interpretation: The given statement whether applies to primary, secondary, tertiary protein structure or not has to be stated.
Concept introduction: The primary protein structure is the order of linking of the amino acids in proteins.
The arrangement of the portion of protein backbone in space gives the secondary protein structure.
The three-dimensional shape of the proteins obtained as a result of the interactions between the amino acid side chains is called the tertiary protein structure.
(c)
Interpretation: The given statement whether applies to primary, secondary, tertiary protein structure or not has to be stated.
Concept introduction: The primary protein structure is the order of linking of the amino acids in proteins.
The arrangement of the portion of protein backbone in space gives the secondary protein structure.
The three-dimensional shape of the proteins obtained as a result of the interactions between the amino acid side chains is called the tertiary protein structure.
(d)
Interpretation: The given statement whether applies to primary, secondary, tertiary protein structure or not has to be stated.
Concept introduction: The primary protein structure is the order of linking of the amino acids in proteins.
The arrangement of the portion of protein backbone in space gives the secondary protein structure.
The three-dimensional shape of the proteins obtained as a result of the interactions between the amino acid side chains is called the tertiary protein structure.
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Chapter 20 Solutions
EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
- Describe the levels of structure of a protein and tell how they would be affected by: a. Hydrolysis with 6M HCl (breaks peptide bond)b. Heating with mercaptoethanol (breaks hydrogen bonds)arrow_forwardWhich 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 endarrow_forwardThe tertiary structure of a protein is established by: a. The sequence of amino acids in the protein b. The molecular weight of the protein c. The total number of amino acids in the protein d. The number of disulfide bridges in the protein e. The net charge of the the protein at physioloical pH.arrow_forward
- A mutation leads to a change in amino acid from valine, an amino acid with a nonpolar side chain, to aspartic acid, an amino acid with a polar, negatively-charged side chain. Do you think that the following levels of protein structure change? If so, how and why? If not, why not? Please frame your answer in terms of chemical bonds and interactions. (primary structure, secondary structure, tertiary structure, quartenary structure)arrow_forwardPhysical methods are often used to determine protein conformation. Describe how x-ray crystallography, cryoelectron microscopy, and NMR spectroscopy can be used to determine the shapes of proteins. What are the advantages and disadvantages of each method? Which is better for small proteins? Large proteins? Huge macromolecular assemblies?arrow_forwardWhich of the following statements are correct about the process of protein structure determination by Cryoelectron Microscopy (Cryo-EM) (select all that apply)? A. Determining a structure by Cryo-EM requires imaging 100s to 1000s of individual protein molecules and using computers to reconstruct 3D images from individual particles B. Requires that proteins form crystals C. Requires freezing of samples to ensure that all proteins are in same orientation D. Requires large quantities of protein to dtermine structure (Typicaly 5-10 ml of 1 mg/ml) E. The raw data obtained by Cryo-EM are 2D images of multiple frozen protein particles.arrow_forward
- Which levels of protein structure are determined by primary structure (i.e. the specific amino acid sequence beginning at the amino terminus of the polypeptide)? Mark all that apply. 1. secondary structure (alpha helices and/or beta sheets) 2. tertiary structure (the folded, three-dimensional shape of a protein) 3. amino acids 4. peptide bondsarrow_forwardWhich of the following statements is true? A. B. C. D. Peptide bonds are the only covalent bonds that can link together two amino acids in proteins. The polypeptide backbone is free to rotate about each peptide bond. Nonpolar amino acids tend to be found in the interior of proteins. The sequence of the atoms in the polypeptide backbone varies between different proteins.arrow_forwardWhich of the following is incorrect? (₁) a. A heterodimer is composed by two identical polypeptide chains b. The polypeptide chains in a multimeric protein are called subunits A homotrimer can be represented with the Greek letter alpha with a sub-index 3 d. Monomeric proteins do not have quaternary structure c.arrow_forward
- Protein folding is critical for function because the properties of a protein arise from its overall shape and the distribution within that shape of the various amino acid side-chains. Which of the following statements about protein three-dimensional structure are correct? 1) the folding pattern of a protein is ultimately determined by its amino acid sequence. 2) proteins tend to fold in such a way that the hydrophobic amino acids are buried in the interior, while hydrophilic amino acids are exposed at the surface. 3) the chemical interactions within a protein molecule that support its overall folded structure are mostly covalent C-C (carbon to carbon) bonds between amino acid side-chains. 4) the overall folding pattern/shape of a protein molecule is termed its primary structure. 5) during evolution, the three-dimensional structure of a protein is often more strongly conserved than its amino acid sequence. More than one answer might be rightarrow_forwardDiscuss the different structures (primary, secondary, tertiary, and Quaternary structures) of protein. What are the five factors that promote protein folding and stability. (Hint: One factor is the Hydrogen bond). Extra Hint: Another factor is the Hydrophobic effect.arrow_forwardIndicate the level(s) of protein structure to which each of the following contributes: a. amino acid sequence b. β-pleated sheet c. hydrogen bond d. disulfide bondarrow_forward
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