BIOLOGY
12th Edition
ISBN: 9781260169614
Author: Raven
Publisher: RENT MCG
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Textbook Question
Chapter 3, Problem 5A
Two different proteins have the same domain in their structure. From this we can infer that they have
a. the same primary structure.
b. similar function.
c. very different functions.
d. the same primary structure but different function.
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Students have asked these similar questions
Which of the following statements is FALSE?
Select one:
a.
Secondary structure of a protein determines how it folds up into a unique three dimensional structure.
b.
Three dimensional structure of a protein determines the function of a protein.
c.
Primary structure of a protein determines how it folds up into a unique three dimensional structure.
d.
Amino acid sequence is absolutely important for a particular protein.
The three-dimensional conformation of a protein may be strongly influenced by amino acid residues that are very far apart in sequence. This relationship is in contrast to secondary structure, where the amino acid residues are:
a. always side by side.
b. generally near each other in sequence.
c. invariably restricted to about 7 of the 20 standard amino acids.
d. often on different polypeptide strands.
e. usually near the polypeptide chain's amino terminus or carboxyl terminus.
Proteins often have regions that show specific, coherent patterns of folding or function. These regions are called:
a. domains.
b.oligomers.
c. peptides.
d. sites.
e. subunits.
Chapter 3 Solutions
BIOLOGY
Ch. 3.1 - Describe the relationship between functional...Ch. 3.1 - Recognize the different kinds of isomers.Ch. 3.1 - Prob. 3LOCh. 3.2 - Prob. 1LOCh. 3.2 - Prob. 2LOCh. 3.3 - Prob. 1LOCh. 3.3 - Prob. 2LOCh. 3.3 - Prob. 3LOCh. 3.3 - Prob. 4LOCh. 3.4 - Prob. 1LO
Ch. 3.4 - Prob. 2LOCh. 3.4 - Prob. 3LOCh. 3.5 - Prob. 1LOCh. 3.5 - Prob. 2LOCh. 3.5 - Prob. 3LOCh. 3 - Prob. 1UCh. 3 - Why are carbohydrates important molecules for...Ch. 3 - Plant cells store energy in the form of ______,...Ch. 3 - Prob. 4UCh. 3 - A molecule of DNA or RNA is a polymer of a....Ch. 3 - Prob. 6UCh. 3 - What monomers make up a protein? a....Ch. 3 - A triglyceride is a form of _______ composed of...Ch. 3 - You can use starch or glycogen as an energy...Ch. 3 - Which of the following is NOT a difference between...Ch. 3 - Prob. 3ACh. 3 - A mutation that alters a single amino acid within...Ch. 3 - Two different proteins have the same domain in...Ch. 3 - What aspect of triglyceride structure accounts for...Ch. 3 - The spontaneous formation of a lipid bilayer in an...Ch. 3 - Prob. 1SCh. 3 - Hydrogen bonds and hydrophobic interactions each...Ch. 3 - Prob. 3S
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- In order to study protein structures and functions, many protein techniques have been developed for specific applications. Which of the following pair of technique: application is INCORRECT? a. Mass Spectrometry: protein molecular weight b. SDS-PAGE: protein structure c. X-ray crystallography: protein structure d. NMR: protein structure e. Peptide mass fingerprinting: protein presence and identificationarrow_forwardWhich of the following is most commonly the rate limiting step in determining the structure of a protein by X-Ray crystallography (select one)? A. Processing collected data B. Collection of data C. Getting crystals of protein D. Expression and purification of protein E. Solving structure from processed dataarrow_forwardOne advantage of the protein structures solved by NMR comparing to the x-ray structures is: a. It can determine the absolute, unique structure. b. It can solve protein structures in solution, which might be more physiological relevant. c. It is much easier to solve the structure. d. It has higher resolution. e. It can solve proteins with higher molecular weight.arrow_forward
- 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 acidsarrow_forwardDenaturation of a protein A. adds hydrogen bonds to the primary level of protein structure. B. breaks hydrogen bonds in the primary level of protein structure. C. adds hydrogen bonds to the secondary and tertiary levels of protein structure. D. breaks hydrogen bonds in the secondary and tertiary levels of protein structure.arrow_forwardA prosthetic group of a protein is a non-protein structure that is: a. a ligand of the protein. b. a part of the secondary structure of the protein. c. a substrate of the protein. d. permanently (tightly) associated with the protein. e. transiently bound to the protein.arrow_forward
- In a protein, a mutation occurs and results in phenylalanine being replaced by an alanine. This would. Select one: a. Always change the primary structure of the protein, never change the tertiary structure of function. O b. Always change the primary structure of a protein, sometimes affect tertiary structure and function. c Never change the primary structure, always affect secondary and tertiary structure and function. O d. Sometimes change the primary structure of a protein, always affect the tertiary structure, and sometimes affect function.arrow_forwardProteins are the dominant structural and functional molecules in a cell. Which one of the following statements about proteins is NOT correct? A. The native conformation of a protein is usually arrived at very quickly after synthesis. B. Hydrogen bonding is the only type of bonding that gives rise to secondary structure. C. Urea denatures proteins by disrupting the interactions among non-polar (hydrophobic) amino acids D. Most proteins consist of a single polypeptide and thus do not have quaternary structure.arrow_forwardBoth 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.arrow_forward
- Which 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_forwardIf I synthesized a protein by chemically linking amino acids together and added a few extra amino acids that made the protein more stable and therefore better at treating a disease, what argument would support a patent for the protein? a. The protein is beneficial to humans and so I should be paid for my discovery. b. The protein is synthetic and different from the natural form. c. The protein was synthesized chemically. d. The protein is expensive to make and a patent would help me offset my costs of production.arrow_forwardIn studying a particular biomolecule (protein, nucleic acid, carbohydrate, lipid), a biochemist needs to separate/ purify it from other biomolecules in the sample. However, looking at the monomeric subunits of a biomolecule, one should have an idea about the characteristics of the molecule that would allow to separate/purify it from other molecules. On what basis can you separate: a. amino acids from fatty acids? b. nucleotides from glucose?arrow_forward
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