attached to the polypeptides keep the amino acid chains in an extended configuration.Membrane proteins of animal cells can have the majority of their polypeptide chainsextending above the plasma membrane surface. Carbohydrate molecules covalentlyThese membrane proteins are examples of:a)b)c)d)lipoproteinsextracellular proteoglycansglycoproteinspeptidoglycansB-barrel proteinsCarbohydrates can be attached tohydroxylysine amino acid residues. Carbohydrates of this type are called:polypeptide chains through serine, threonine, orglycosaminoglycansO-linked oligosaccharideslipopolysaccharidesO-antigensN-linked oligosaccharidesa)b)

Biomolecules are organic molecules that take part in various biochemical reactions. These are mainly…

Answered: attached to the polypeptides keep the…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

Terpenes are a class of lipids based on the isoprene molecule and are typically incorporated into complex molecular structures. Which of the following molecules 3. a) b) retinal vitamin K vitamin E phosphatidic acid coenzyme Q lonile The steroids are lipids with a variely of different functions in cells that have structures based upon the steroid nucleus. Sterolas that have cholesterol as a precursor but do not function as hormones include: a) myristic acid, palmitic acid b) glucocorticoids, mineralocorticoids tristearoylglycerol, trioleoylglycerol cholic acid, deoxycholic acid sphingomyelins, glycosphingolipids c) d) e)
Which of the following (could be more than one) would not be a rational explanation for why the three-dimensional structure of a protein is driven and stabilized largely by noncovalent rather than covalent bonds?a) Proteins may be degraded for energy, and if their three-dimensional structures were heldtogether by mostly covalent bonding, this might be too difficult to accomplishb) Proteins will need to be unfolded to cross biological membrane, and if their three-dimensionalstructures were held together by mostly covalent bonding, this might be too difficult toaccomplish.c) Protein function (transport, enzyme catalysis, etc...) may require flexibility in the three-dimensional structure to allow for conformational change, and if protein three-dimensionalstructure were held together by mostly covalent bonding, this might be too difficult toaccomplish.d) All of the answer choices are rational explanations for why the three-dimensional structure of protein is driven and stabilized largely…
Describe, The negatively charged glycosaminoglycan polysaccharide chains establish a hydrated gel-like environment around the cell.
Describe the macromolecular and biophysical characteristics of collagen in the extracellular matrix (ECM). How does the molecular composition of collagen impact these characteristics?
Proteoglycan aggregates in tissues form hydrated, viscousgels. Can you think of any obvious mechanical reason whytheir capacity to form gels is important to cell function?[Hint: Liquid water is virtually incompressible.]
Compare the structure of proteoglycans and glycoprotein. How are structural differences related to their function
Match each of the statements below with the fibrous protein that mostly fits the description. Coiled-coil of alpha helices V [ Choose] Collagen Silk fibroin Keratin Triple helical arrangement of polypeptide chains Extended anti-parallel beta sheets [ Choose ] Characterized by a predominant (GSGAGA)n repeat in the primary seguence [ Choose] Found in hair, feathers, scales, and nails [ Choose ] Is produced by insects and spiders [ Choose ] The sequence Gly-Pro-Hyp occurs frequently in this fibrous protein [ Choose ] Is characterized by the heptad pseudo- [ Choose ] repeat Major component of skin, tendons, ligaments and teeth [ Choose ] Characterized by regular inter-sheet spacing [ Choose ] of 0.35 and 0.57 nm
Biological membranes are critical components of cells that allow compartmentalisation of cellular contents. The diagram shows a biological membrane comprised of a lipid bilayer with a single polypeptide integrated into the membrane and spanning the membrane seven times. What types of amino acids are likely present in the parts of the polypeptide chain labelled 1-7 and in the parts of labelled A-G? What is the name of the effect that forces the polypeptide to arrange itself like this within the lipid bilayer? Give an example of a type of molecule that can move freely across the lipid bilayer and explain why it can do so based on its chemical properties.
Although proteins rarely if ever flip-flop across a membrane, the distribution of membrane lipids between the membrane leaflets is not absolute except for glycolipids. Why are glycosylated lipids less likely to flip-flop?
g) Describe the biological function of the peptide hormone insulin. h) Haemoglobin is an example of a quaternary protein. Briefly describe the structure of this protein and state its biological function.
Proper folding is essential for most proteins to function. Which of the following statement about protein folding are correct. There may be more than 1 right answer. a) changing the primary sequence will change the final conformation b) desaturation results in a protein that has a higher free energy than the native conformation c) protein spontaneously fold into their correct shape d) denatrutation will cause a protein to lose its tertiary structure
Describe the two types of secondary structure apolypeptide can attain. Which proteins can achievequaternary structure? Which protein structure(s) are alteredby denaturation?

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