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Unstructured proteins A. are those proteins that have been denarured by heat. B. do not have any biological functions. C. can be induced to have a defined structure by binding to other proteins or to DNA or RNA. D. have no secondary or tertiary structure. E. have regions that are very rich in aromatic amino acids.

Short Answer

Expert verified
Answer: Unstructured proteins can sometimes acquire a specific structure when they interact with other biomolecules.

Step by step solution

01

Understand Unstructured Proteins

To answer the question, we have to understand what unstructured proteins are. Unstructured proteins are proteins that do not have a well-defined, rigid three-dimensional structure, including secondary and tertiary structures. They are also known as intrinsically disordered proteins. These proteins can sometimes acquire a specific structure when they interact with other biomolecules, and they are known to have certain biological functions.
02

Analyze Each Option

Let's evaluate each option in the question to determine the most accurate definition of unstructured proteins: A. Unstructured proteins are not necessarily denatured by heat. Denatured proteins are proteins that have lost their native structures due to any kind of disruption, such as heat, pH, or chemical agents. B. This statement is incorrect. Unstructured proteins do have biological functions. They are often involved in signaling pathways and protein-protein interactions. C. This statement is correct. Unstructured proteins can sometimes acquire a specific structure when they interact with other biomolecules such as proteins, DNA, or RNA. D. Unstructured proteins do not have a well-defined, rigid three-dimensional structure, but they can still have some local secondary structures. This statement is partially true, as it says that unstructured proteins have no secondary or tertiary structure. Unstructured proteins can have local secondary structures (such as alpha-helixes and beta-sheets), but they generally lack a well-defined tertiary structure. E. Unstructured proteins do not necessarily have regions that are very rich in aromatic amino acids. This description does not define unstructured proteins accurately.
03

Choose the Correct Answer

Based on our analysis of each given statement, option C is the most accurate definition of unstructured proteins. Unstructured proteins can be induced to have a defined structure by binding to other proteins or to DNA or RNA.

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Most popular questions from this chapter

Abnormalities in the synthesis or structure of collagen cause dysfunctions in cardiac organs, bone, skin, joints, and cyes. Problems may result from abnormal collagen genes, abnormal posttranslational modifications of collagen, or deficiency of cofactors needed by enzymes responsible for posttranslational modifications. Scurvy, a lack of vitamin \(\mathrm{C},\) is an example of the last type. The formation of covalent cross-links in collagen A. occurs during synthesis of the peptide chain. B. uses hydroxyproline. C. involves glycine residues. D. requires conversion of some \(\varepsilon\) -amino groups of lysine to \(\delta\) -aldchydes. E. all of the above.

Many pathological hyperlipoproteinemias result from abnormalitics in the rates of synthesis or clearance of lipoproteins in the blood. They are usually characterized by elevated levels of cholesterol and/or triacylglycerols in the blood. Type I has very high plasma triacylglycerol levels \((>1000 \mathrm{g} / \mathrm{dL})\) because of an accumulation of chylomicrons. Type II (familial hypercholesterolemia) has elevated cholesterol, specifically in the form of LDL. Another abnormality of lipoproteins is hypolipoproteinemia in which lipoproteins are not formed because of the inability to make a particular apoprotein. All lipoprotein particles in the blood have the same general architecture which includes A. a neutral core of triacylglycerols and cholesteryl esters. B. amphipathic lipids oriented with their polar head groups at the surface and their hydrophobic chains oriented toward the core. C. most surface apoproteins containing amphipathic helices. D. unesterificd cholesterol associated with the outer shell. E. all of the above.

Many pathological hyperlipoproteinemias result from abnormalitics in the rates of synthesis or clearance of lipoproteins in the blood. They are usually characterized by elevated levels of cholesterol and/or triacylglycerols in the blood. Type I has very high plasma triacylglycerol levels \((>1000 \mathrm{g} / \mathrm{dL})\) because of an accumulation of chylomicrons. Type II (familial hypercholesterolemia) has elevated cholesterol, specifically in the form of LDL. Another abnormality of lipoproteins is hypolipoproteinemia in which lipoproteins are not formed because of the inability to make a particular apoprotein. In abecalipoproteinemia chylomicrons, VLDL and LDL are absent from the blood. Which of the following is correct? A. In this discase, no apolipoproteins are synthesized. B. If the blood from these individuals were centrifuged, the lipid bands would be found primarily in the upper half of the tube. C. Failure to synthesize apolipoprotein ApoB-100 and ApoB-48 would account for the pattern shown in this disease. D. Apolipoproteins are composed mostly of \(\beta\) structure. E. All of the above.

In an \(\alpha\) -helix, A. side-chain groups can align to give a polar face. B. cach peptide bond forms two hydrogen bonds. C. there are 3.6 amino acids per turn. D. all of the above. E. none of the above.

Proteins may be separated according to size by A. isoclectric focusing. B. polyacrylamide gel electrophoresis. C. ion exchange chromatography. D. molecular exclusion chromatography. E. reverse-phase HPLC.

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