2Keratin is a type offound in thecytosol, which means its hydrophobic amino acids areSelect one:b.O c.a. amino acid, skin, exposed on the surface of the proteinprotein, hair, exposed on the surface of the proteinprotein, liver, exposed on the surface of the proteinprotein, liver, not exposed on the surface of the proteine. protein, hair, not exposed on the surface of the proteinO d.Lue Dec 8 at 5pmof humans. On a cellular level, keratin is found in theJump to...45Next page

Keratin is a type of protein that is also known as scleroprotein. This protein is present in hairs.…

Keratin is a type of found in the cytosol, which means its hydrophobic amino acids are Select one: of humans. On a cellular level, keratin is found in the a. amino acid, skin, exposed on the surface of the protein protein, hair, exposed on the surface of the protein O b. c. protein, liver, exposed on the surface of the protein O d. protein, liver, not exposed on the surface of the protein O e. protein, hair, not exposed on the surface of the protein

Keratin is a type of found in the cytosol, which means its hydrophobic amino acids are Select one: of humans. On a cellular level, keratin is found in the a. amino acid, skin, exposed on the surface of the protein protein, hair, exposed on the surface of the protein O b. c. protein, liver, exposed on the surface of the protein O d. protein, liver, not exposed on the surface of the protein O e. protein, hair, not exposed on the surface of the protein

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter3: Biological Macromolecules

Section: Chapter Questions

Problem 2VCQ: Figure 3.23 Which categories of amino acid would you expect to find on the surface of a soluble...

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A C2 G This a photograph of an actual polyacrylamide gel that has been run with samples of protein. For each question, write the letter from the item in the gel that best matches the word or concept that is described. Answers may be used once, more than once, or not at all. There may be more than one correct answer per question. 1. Band 2. Lane 3. Well 4. Will protein migrate through the gel from A to B or will it migrate from B to A? 5. Which end is nearest the negative electrode, A or B? 6. Which contains smaller protein fragments, F or G? 7. Which letter indicates the highest concentration of protein fragments that are the same size 8. Where would a sample of protein be loaded? B.
Which of the following about protein denaturation is not trueA. It is always irreversible B. It is a shape change C. It may be due to pH / temperature change D. Most of the proteins denature when transferred from aqueous environment to organs solvents E. Its function is lost.
Which of the following is incorrect about the beta sheet? Parallel beta sheets are less stable than the anti-parallel ones O b. It is stabilized by hydrophobic interactions between the side chains O c. The strands in anti-parallel beta sheets are usually connected with turns O d. Side chains of residues are alternated above and below the sheet a.
S1.What functional group (pictured below) is used in the formation of ATP, the backbone of DNA, and the plasma membrane? R. - HO- asluolom OgH 910m ansa obyd to inuoms adisi69 101 P- Hnedenoi HO 9tom anisinos H 19w 1639 eniv blut viend ou nontel:oceansied bol-ngtsl s19 1591 a. Amino b. Carbonyl c. Ester d. Phosphate e. Alcohol Sabios onime Tertio of bensemoo Insietib ti aolem tsrll blas onims ns to neg at to quang ly snodibod for ogh quotg
which of the following is correct about protein hydration? a- hydrophobic pathces are hydrated first followed by exposed polar side chains. b- the monolayer water that hydreates proteins are those that hydrate ionic, polar, and nonpolar amino acids on the surface of the protein c- polar amino acids are the first hydrated followed by ionic aminio acids d- hydration of hydrophoic patches in proteins is not possible
+H₂N-CH-COO™ 1 CH₂ I CH₂ 1 CH₂ I +H₂N-CH₂ A. O amino acid B amino acid D amino acid A amino acid E +H₂N-CH-COO™ 1 CH₂ T O amino acid C CH₂ 1 C=0 B. This amino acid participates in hydrophobic interactions to stabilize protein conformation. +H₂N-CH-COO™ I CH₂ I OH C. +H₂N-CH-COO™ I CH H₂C CH3 D.
Figure 3.23 Which categories of amino acid would you expect to find on the surface of a soluble protein, and which would you expect to find in the interior? What distribution of amino acids would you expect to find in a protein embedded in a lipid bilayer?
Denaturation is the loss of protein function from structuralchange or chemical reaction. At what level of proteinstructure or through what chemical reaction does each ofthe following denaturation agents act?a. heatb. strong acidc. saturated salt solutiond. organic solvents (e.g., alcohol or chloroform)
What can be deduced from the following information? N- C- Protein Nonpolar polar acidic basic term term 33 42 10 15 Ser Asp Y 33 42 10 15 Ser Asp A. The two proteins, X and Y are one and the same B. The two proteins are globular proteins that are hydrophilic C. The two proteins are most likely localized in the cytoplasm D. X and Y most likely have transport function for various types of metabolites E. The data is inconclusive and similarity or differences between X and Y cannot be determined
When a protein is folded in aqueous solution, some residues are driven inside to form a “hydrophobic core” which is far away from the water molecule. Which pair of the following residues are likely to be in the “hydrophobic core”? a. Gln and His b. Thr and Val c. Asp and Arg d. Ser and Tyr e. Ile and Leu
Which of the following is incorrect about the beta-sheet? a. The strands in anti-parallel beta-sheets are usually connected with turns b. Side chains are alternated above and below the sheet C. Parallel beta-sheets are less stable than the anti-parallel ones Od. It is stabilized by hydrophobic interactions between the side chains of nonpolar residues
The function of a protein depends on ... . and the 3D shape of a protein is controlled by Select one: ut of O a. Its ability to recognize certain substances, Primary structure O b. Its ability to resist temperature, Secondary structure uestion c. Its ability to resist pH, Quaternary structure O d. Its ability to recognize specific substances, Tertiary structure O e. Its ability to bind to many molecules, Secondary structure