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 The strands in anti-parallel beta sheets are usually connected with turns Od. Side chains of residues are alternated above and below the sheet O c. a.

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 The strands in anti-parallel beta sheets are usually connected with turns Od. Side chains of residues are alternated above and below the sheet O c. a.

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter3: Biological Molecules: The Carbon Compounds Of Life

Section: Chapter Questions

Problem 8TYK: The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices...

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A protein has a clearly defined hydrophobic core; however there is the residue glutamine within the hydrophobic core. How is this residue most likely stabilized (aka ‘made happy’) within this hydrophobic core? a. Hydrophobic interactions b. Interactions with a metal ion c. Hydrogen bonds d. Ionic interactions e. Electrostatic interactions
You are treating your bacteria with an antibiotic that binds to the D-ala-D-ala stucture of the peptide side chain (literally sits right on top of that D What happens due to the antibiotic binding? O A. Racemase cannot cross link peptide side chains • B. Peptide side chain are not added to NAM • C. Glycosidic bonds between NAM and NAG do not form D. Bactoprenol cannot move the dissacharide submit to the extrenal side of the membarne • E. Transpeptidase cannot cross-link peptide side chains
The β-Sheet is formed mainly by a. hydrophobic interaction b. hydrogen bonding between the peptide bond and water c. hydrogen bonding between two strands d. hydrogen bonding of the side chains e. disulfide bonding
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.
Beta-sheets form through ___ between ___. a hydrogen bonds; groups on the polypeptide backbone b hydrogen bonds, ionic bonds, and hydrophobic forces; groups on the polypeptide backbone c hydrogen bonds; backbone groups and side chains d hydrogen bonds, ionic bonds, and hydrophobic forces; backbone groups and side chains
The pKa of the Histidine side chain is 6.0. When Histidine is dissolved in a buffer with pH 5.0, the side chain is a. neutral without net charge b. more hydrophobic c. negatively charged d. positively charged
Which of the following is FALSE? Select one: a. The hydrogen bonding in a beta-sheet is between strands rather than within strands. b. The two main types of secondary structure are the alpha-helix and beta-sheet structures c. The hydrogen bonding in a beta-sheet is within strands rather than between strands. d. Alpha-helix is maintained by hydrogen bonds.
Which of the following is true regarding proteins A. Absorbance of proteins is directly proportional to the molecular weights B.Proteins react with biuret reagent because of their side chains C. two out of the twenty amino acids can absorb at 280nm D. In proteins the average weight per amino acid residue always varies
Proteins denature at low pH. What characteristic of acidic environments interferes with protein folding? A. The lack of protons in the solution breaks covalent bonds in the protein. B. The excess protons in the solution break covalent bonds in the protein. C. The lack of protons in the solution breaks hydrogen bonds in the protein. D. The excess protons in the solution break hydrogen bonds in the protein.
Which of the following statements are true about stacking and separating gels? a. The holes is the separating gel are much smaller than the ones in the stacking gel. b. The stacking gel is at a pH of 6.9, while separating gel is at a pH of 8.9 c. The higher pH in separating gel causes the glycine buffer to accelerate more and thus leaving behind the proteins to stack at the interface. d. The smaller holes in separating gel slows down the mobility of the proteins at the interface.
Tertiary structure of protein is maintained by Select one: a. Hydrogen bond b. All of these c. Di-sulphide bond d. Peptide bond
In order for proteins to function properly the neccessary amino acids must have a specific what? A. Sequence B. Bond C. Number D. Compound