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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EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
- 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_forwardWhich of the following types of molecular interactions play a role in protein folding? Select all that apply. A.)Hydrophobic interactions B.)Van der Waals attraction C.)Hydrogen bonds D.)Covalent bondsarrow_forwardPhysical methods are often used to determine protein conformation. Describe how x-ray crystallography, cryo electron 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_forward
- 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_forwardDescribe how a polypeptide can fold to become a functioning protein. Be sure to address the four levels of protein (folding or organization known as hierarchy of structure). In addition, describe three different jobs proteins can perform if the protein has the correct shape.arrow_forward
- Which 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_forwardProteins undergo  a process, called folding to establish their final, functional configuration. Amino acids them selves are covalently, bound to gather, but for other forces are needed to maintain a functional proteins structure. Briefly describe these forces.arrow_forwardMatch the level of protein structure to its description: Primary Secondary Tertiary Quaternary A. Folding due to interactions among the peptide backbone B. Interactions among multiple polypeptide chains C. Sequence of amino acids D. Folding due to interactions among side chainsarrow_forward
- Choose one for each question given: A. quaternary level B. tertiary level C. primary level D. secondary levelarrow_forwardWhich 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 paarrow_forwardWhich of the following statements is incorrect? A.- the structure and charge of the proteins have direct effects on the rate of its migration through the gel matrix include b.- SDS is a type of a buffer with strong protein-denaturing effect and binds to the protein backbone at a constant molar ratio c.- SDS and polyacrylamide gel largely eliminates the influence of the structure and charge, and proteins are separated solely based on polypeptide chain length. d.When proteins are separated by electrophoresis through a gel matrix, smaller proteins appears at the lower portion of the gelarrow_forward
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