Which of the following regarding disulfide bonds is/are true? Disulfide bonds are the most common intrachain covalent linkage in proteins Disulfide bond formation is critical for correct protein folding into the native conformation Disulfide bonds impart a large degree of stability to the secondary structure of proteins The intracellular environment is too oxidizing to allow disulfide bond formation A and D
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- Which of the following is the TRUE statement? When found together, a helices and B sheets are generally found in the same structural 'layer The B conformation is most stable when the individual segments are twisted in a left-handed direction Hydrophobic interactions make a large contribution to the stability of protein structures, therefor, burial of hydrophobic amino acid residues need at least two layers of secondary structure The backbone segment of a ß conformation polypeptide segment can readily H-bond to an a helix adjacent to itGive the force of interaction involved in the protein folding of the protein structure A and C: COO CH,C-N-H• • •0- Pleated sheet structure A H C Helical structure CH3 CH3 - CH3 -CHCH,CH, CH- CH, CH3 (CH,),NH, -0-CCH,- C=0..•HN CH, CH, CH,CH CH,CH CH, CH, CH OH 0=C -CH,-S,S-CH,- H,Ñ Structure A: H-bonding: Structure C: Van der Waals O Structure A: Covalent interaction; Structure C: dipole-dipole interaction O Structure A: Salt bridge: Structure C: H-bonding Structure A: Hydrophobic interaction; Structure C: ionic interaction 00000 BChicken egg contains a lot of proteins which supports the growth and development of the chicken embryo. The chicken egg was placed on high heat (100°C) until it forms a solid structure. Which of the following statements is correct about the given scenario? O The increase in temperature may interfere intermolecular forces of attraction that stabilizes the native conformation. O Structural and functional characteristics of proteins remain intact even temperature was increased to boiling O Extreme temperature conditions may result to irreversible denaturation due to destruction of primary. secondary, tertiary, and quaternary structures By decreasing the temperature, the egg embryo can still develop, and grow to become a chicken because renaturation may take place.
- Why might adding a strong reducing agent like Dithiothreitol (DTT) help denature an extracellular protein? O Disulfide bonds might be reduced that might be critical in stabilizing its structure O Disulfide bonds might be oxidized that might be critical in stabilizing its structure O Disulfide bonds formed inside the cytoplasm can be oxidized O Cysteines can be reduced to form stabilizing disulfide bondswhich 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 possibleWhich of the following factors do not stabilize the 3-D structure of a folded protein? O Disulfide bonds O Van der Waals interactions O Hydrogen bonds O Electrostatic interactions O Hydrophobic bonds Metal-ion protein interactions
- When a protein folds into a quaternary structure the outside amino acids are exposed to the aqueous (water rich) environment. These amino acid R likely have what chemical properties? O The amino acid R groups are polar and hydrophilic The amino acid R groups are non-polar and hydrophobic O The amino acid R groups have hydrocarbon functional groups O The amino acid R groups have unreactive functional groupsThe R-group of lysine has an overall positive charge. The R-group of glutamic acid has an overall negative charge. Within the structure of a protein molecule, these two amino acids will: O attract each other O repel each other O form a disulfide bridge O form a pure covalent bondHydrogen bonds that form a helices and B-pleated sheets are the primary interaction in which level of protein structure? O secondary O quaternary O primary O tertiary
- There is a "primary driving force" behind protein folding (to form tertiary structure). This driving force can be used to explain below phenomenon except: water has a high density and a high boiling temperature non-polar amino acids go inside a protein long chain fatty acids form micelles oil spills go to the surface of water phospholipids form lipid bilayerch one of the following statements about protein structure is NOT correct? . Domains are discrete parts of a protein structure, usually associated with a particula function. true Beta-sheets are stabilised by hydrogen bonds between amino-hydrogens and carbonyl-oxygens from peptide bonds. no adjacent hydrogen bonding Proteins made from three polypeptide chains show quaternary structure. Yes Smaller protein domains come together to from supersecondary structures and moPart A What is the highest structural level of protein structure represented in the following image? primary quaternary secondary pentanary tertiary O O