Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Chapter 12, Problem 10P
Interpretation Introduction
Interpretation:
The reason for the glycosylated lipids to be lesslikely to flip-flop needs to be explained.
ConceptIntroduction:
In addition to galactose, they start an energy barrier to flip-flop. This energetic barrier improvesthe irregularity of the membrane. The addition of carbohydrates significant energy barrier to the flip-flop.
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structure. They provide the matrix or ground substance of extracellular tissue spaces in
which collagen and elastin fibers are embedded. Hyaluronic acid, chondroitin 4-sulfate,
heparin, are among the important glycosaminoglycans.
10. Glycoproteins are a group of biochemically important compounds with a variable
composition of carbohydrate (1-90%), covalently bound to protein. Several enzymes,
hormones, structural proteins and cellular receptors are in fact glycoproteins.
Chapter 2: CARBOHYDRATES
SELF-ASSESSMENT EXERCISES
I. Essay questions
1. Define and classify carbohydrates with suitable examples. Add a note on the functions of
carbohydrates.
2. Describe the structure and functions of mucopolysaccharides.
3. Give an account of the structural configuration of monosaccharides, with special reference to
glucose.
4. Discuss the structure and functions of 3 biochemically important disaccharides.
5. Define polysaccharides and describe the structure of 3 homopolysaccharides.
III. Fill…
Part I. Protein structure
You have the toy model for a protein in the water (W) environment
of the cell shown.
a) How many residues (amino acids) does this toy protein have?
b) How many hydrophobic (H), hydrophilic (P), and charged (C)
residues are there?
c) Sketch the molecule on your answer sheet and then show the
positions of the favorable C-C (charge-charge) interactions
on the figure.
messengeRsand transpor
and share
materes
2. Now think about the bilayer arrangement of phospholipids in cell membranes. Imagine if
extracellular and intracellular fluids were made of oil instead of water. How would the phospholipids
arrange themselves?
A. The hydrophilic heads would be oriented toward the middle, with hydrophobic tails
pointing outward.
B. The hydrophobic heads would be oriented toward the oil, so outward; the hydrophilic tails
would be pointed inward.
C. The hydrophobic tails would be oriented inward, while the hydrophilic heads would point
outward.
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Protein Structure and Function A common strategy in the regulation of protein function is to alter its structure. Describe two specific strategies used by the cell to alter a protein’s structure, thereby altering its function.arrow_forward(a). Phospholipids are amphipathic molecules which have hydrophilic and hydrophobic regions. Explain how this feature benefits the cell. (Give ONE reason) (2) (b). Give ONE difference between a saturated phospholipid and an unsaturated phospholipid. (2)arrow_forwardCreate a ROUGH SKETCH (no need for exact hydropathy indices and residue numbers) of the hydropathy plot for the given membrane protein. -coo Please follow the color assignment of the helical domains and properly label the plot and axes. Here is an example: Amino Outside terminus Transmembrane helices are predicted by hydrophobic stretches of 20-25 aa residues 10 50 100 150 200 250 Hydrophobic Inside Hydrophilic Carboxyl terminus -3 10 50 100 150 200 250 Residue number Bacteriorhodopsin Hydropathy indexarrow_forward
- R V. Phospholipids are the main structural lipids that comprise cellular and organellar membranes. One abundant phospholipid in bacterial cell membranes is phosphatidylethanolamine (PE), which has a generic structure shown on the right. Note that R1 R and R2 are representative alkyl chains of attached fatty acids, each having about 16 – 20 carbon atoms. a) The overall net charge in one PE molecule is: -2 -1 0 +1 +2 CH₂ Phosphatidylethanolamine (PE) -CH H₂C. b) The glycerophosphate backbone in PE is a: D-enantiomer c) The fatty acids are attached to PE via which type of bond? amine L-enantiomer racemic NH3 amide ester ether d) Draw the commonly used cartoon representation of one phospholipid molecule. Label the hydrophilic and hydrophobic parts.arrow_forward7 Protein structure.Circle one of the three amino acid sequences that is most likely to form a stable a-helix? RASKTARQ DASKTAEQ KPGKPAGQ In one sentence (that can be accompanied by a small picture) explain why?arrow_forwardHydropathy & Amphipathicity 2 -1 -2- 110 210 310 410 510 Residue Number C. Draw the topology of this membrane protein in the bilayer and indicate the range of residues forming transmembrane a-helices.arrow_forward
- Shape and dimension. (a) Tropomyosin, a 70-kDa muscle protein, is a two-stranded α-helical coiled coil. Estimate the length of the molecule. (b) Suppose that a 40-residue segment of a protein folds into a two-stranded antiparallel β structure with a 4-residue hairpin turn. What is the longest dimension of this motif?arrow_forwardstructure of cholesterol, define the three regions of the molecule, know that this molecule regulates membrane fluidity, and distinguish between esterified and unesterifiedcholesterolarrow_forwardPlease help me with this question. More than one answer may be correct. Elastin _______. Options: A) has a repeating structure of 3 amino acids such as Gly-Pro-X B) crosslinks with numerous other elastin peptides to make an elastic fiber C) is physically attached to the smooth endoplasmic reticulum D) is physically attached to ribosomes E) is rich in hydrophobic residuesarrow_forward
- Roughly sketch the hydropathy plot for the given hypothetical membrane protein. Follow the color assignment of the helical domains and properly label your plot and axes (NB: Only a rough sketch is being asked. No need be exact with the hydropathy indices and residue numbers). CO-arrow_forward. Consider a small protein containing 101 amino acid residues. The protein will have 200 bonds about which rotation can occur. Assume that three orientations are possible about each of these bonds. (a) Based on these assumptions, about how many random-coil conforma- tions will be possible for this protein? (b) The estimate obtained in (a) is surely too large. Give one reason why.arrow_forwardProtein Concept Map Add these terms to your concept map should include these concepts and details: Structure (functional groups, shape); Monomer; Linkage; Properties; Functions; Key terms from the Partial List of Key Terms from the Minds Partial List of Key Terms essential amino acid amino acid side group/R-group peptide bond polypeptide receptor neurotransmitter hormone secondary structure tertiary structure quaternary structure fair test hydrophobic hydrophilic intermolecular force of attractionarrow_forward
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