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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.

Short Answer

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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. unesterified cholesterol associated with the outer shell E. all of the above Answer: E. all of the above

Step by step solution

01

Option A: a neutral core of triacylglycerols and cholesteryl esters

Chylomicrons, Very Low-Density Lipoprotein (VLDL), Low-Density Lipoprotein (LDL), and High-Density Lipoprotein (HDL) are the main lipoprotein particles in the blood. All of these particles have a neutral lipid core containing triacylglycerols and cholesteryl esters, which is surrounded by a shell of amphipathic lipids and proteins. #Step 2: Analyzing option B#
02

Option B: amphipathic lipids oriented with their polar head groups at the surface and their hydrophobic chains oriented toward the core

The lipoprotein particles are surrounded by a shell, consisting mainly of phospholipids. These amphipathic lipids orient themselves with their polar head groups at the surface and their hydrophobic chains toward the neutral core. This orientation ensures the stability and solubility of lipoprotein particles in the blood. #Step 3: Analyzing option C#
03

Option C: most surface apoproteins containing amphipathic helices

Apoproteins (or apolipoproteins) are present on the surface of lipoprotein particles and normally have an amphipathic helix structure, which ensures stable interactions with the lipids of the shell and the neutral lipid core. These proteins provide structural stability and play a role in the metabolism and transport of lipids in the blood. #Step 4: Analyzing option D#
04

Option D: unesterified cholesterol associated with the outer shell

Unesterified cholesterol molecules are also present in the outer shell of lipoprotein particles. They are attracted to the outer hydrogen atoms of the amphipathic lipids, contributing to the stabilization of the lipoprotein structure and its solubility in the blood. #Step 5: Identifying the correct option#
05

Correct option: E. all of the above

Based on the analysis in steps 1-4, it is evident that all of the given options correctly describe the general architecture of lipoprotein particles in the blood. Thus, the correct answer is E. all of the above.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Hyperlipoproteinemias
When delving into the complexities of hyperlipoproteinemias, it is essential to recognize that these conditions represent an array of disorders linked to abnormal levels of lipoproteins, which include both cholesterol and triacylglycerols, within the blood. These disorders may arise from variances in the speed at which these lipoproteins are synthesized or cleared from the bloodstream.

For instance, Type I hyperlipoproteinemia is notably marked by a significant increase in plasma triacylglycerol levels due to the build-up of chylomicrons. Type II, often termed familial hypercholesterolemia, is characterized by elevated low-density lipoprotein (LDL) cholesterol. This knowledge can enhance a student's understanding by showcasing concrete examples of how these complex conditions differ and affect the body.
Lipoprotein Structure
Understanding the structure of lipoprotein particles is crucial for students delving into the intricacies of lipid transport and metabolism. At the core of each particle lies a neutral cluster of triacylglycerols and cholesteryl esters, forming the hydrophobic center. Surrounding this core is a meticulously organized layer of amphipathic lipids. These molecules are characterized by their polar head groups that face the watery environment of the blood and their nonpolar tails that extend inward, aligning with the lipid core.

By grasping this architectural blueprint, students can better internalize how the structure allows lipoproteins to remain soluble in the bloodstream, facilitating the distribution of lipids to various body tissues.
Cholesterol and Triacylglycerols
The roles of cholesterol and triacylglycerols within lipoproteins are central to understanding lipid metabolism. Cholesterol, particularly when unesterified, is a core component of the exterior shell of lipoprotein particles, contributing to their stability and fluidity. Triacylglycerols, or triglycerides as they are commonly known, reside mainly in the particle's inner core alongside cholesteryl esters and are the primary form of transported fat in the blood.

These lipids are crucial for the production of energy and the synthesis of certain hormones and vitamin D. Educating students on the importance of these molecules not only in lipoproteins but also in overall bodily functions can solidify their grasp on how disturbances in their levels can influence health.
Apolipoproteins
Lastly, a closer examination of apolipoproteins sheds light on their indispensable role in lipoprotein function. These proteins envelope the lipoproteins and serve numerous purposes, such as assisting in the structural integrity of the lipoprotein particles and playing a crucial part in their recognition by cell receptors, thus directing their metabolism. Apolipoproteins are key players in signaling pathways that determine lipid clearance or delivery and are integral in governing the interactions of lipoproteins with enzymes and cell surface proteins.

Highlighting the variety and functionality of apolipoproteins can aid students in appreciating how alterations in these proteins might result in various lipid disorders, including hyperlipoproteinemias and hypolipoproteinemias.

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Most popular questions from this chapter

Similar arrangements of secondary structural motifs are often observed in the fold structure of protein domains. Which of the following is correct? A. Superfolds are similar structures from proteins related by function or evolution from the same primordial gene. B. Folds must be either all \(\alpha\) or all \(\beta\) C. There is only one type of \(\beta\) domain. D. If a protein has more than one domain, all domains are identical. E. A common fold has a central \(\beta\) -barrel with the strands connected by \(\alpha\) -helices around the outside.

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.

After purification, the Edman reaction was used to sequence a dodecapeptide, yielding the following data: the C-terminal amino acid is isolcucine; the N-terminal amino acid is methionine; and the peptide fragments are Ala-Ala- Ile, Leu-Arg-Lys-Lys-Glu-Lys-Glu-Ala, Met-Gly-Leu, and Met-Phe-Pro-Met. What is the sequence of this peptide?

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.

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. In collagen: A. intrachain hydrogen bonding stabilizes the native structure. B. three chains with polyproline type helical conformation can wind about one another to form a superhelix because of the structure of glycine. C. the \(\varphi\) angles contributed by proline are free to rotate. D. regions of superhelicity comprise the entire structure except for the \(N\) - and \(C\) -termini. E. crosslinks berween triple helices form after lysine is converted to allysine.

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