Which of the following types of bonds are present in the primary structures of proteins? O Hydrogen bonds and covalent bonds Covalent bond Covalent bonds, hydrogen bonds and dislufide linkages O lonic interactions
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- Question 4 Which of the following best describes the formation of the tertiary structure of a protein? A B с D The sequence of the amino acids in the polypeptide chain has no effect on the tertiary structure of the protein. The interactions between the R groups in the polypeptide directly determine the tertiary structure of the protein. The dehydration reaction that covalently bonds the amino acids in the polypeptide di- rectly determines the tertiary structure of the protein. The number of amino acids in the polypeptide directly determines the tertiary structure of the protein.Question 13 What determines protein conformation? all of these O a polypeptide chain of a particular amino acid sequence O interactions responsible for additional structures physical condition of environment chemical condition of environmentQuestion 3 of 3 > r: te e Select the true statements about protein secondary structure. IS IS In a B-pleated sheet, the side chains are located between adjacent segments. Peptide bonds stabilize secondary structure. The secondary level of protein structure refers to the spatial arrangements of short segments of the protein. In an a-helix, the side chains are located on the outside of the helix. The a-helix is held together by hydrogen bonds between the amide N-H and C=0 groups. earning, Inc. privacy policy terms of use contact us help about us careers 112 30 FEB 2 4.
- QUESTION 30 Which of the following is a correct monomer/polymer pairing? O a. monosaccharide + monosaccharide + H2O = disaccharide O b. monosaccharide + monosaccharide= disaccharide + H2O O c. disaccharide monosaccharide + monosaccharide +H2O O d. disaccharide + H2O = monosaccharide + monosaccharide Click Save and Submit to save and submit. Click Save All Ansurers to save aQuestion 1Predicting Secondary Structure Which of the following peptides is more likely to take up an -helical structure, and why? (a) LKAENDEAARAMSEA (b) CRAGGFPWDQPGTSNQuestion 22: which of the following secondary structures would you expect to find on the surface of a globular protein? Alpha helix Beta sheet Loops between two alpha-helices None of the above because water would disrupt the hydrogen bonding that stabilizes these structures A,B and C as long as the polar and charged amino acid side chains face the surface of the protein.
- QUESTION 4 Which of the following amino acids would stick to a CM-sepharose column at pH 7.07 Choose all that apply. Partial credit is allowed for each correct answer, arnd negative scores are allowed for incorrect answers. O Arginine (pl -10.76) O Glutamic acid (pl 3.22) O Cysteine (pl 5.07) O Histidine (pl 7.59)Question 4. Imagine the main chain of a protein bends back on itself so that two amino acid residues R1 and R2 come close to each other. In the table below are four possibilities for what R1 and R2 might be. In each case, decide whether a specific interaction could form between the residues. If a specific interaction could form, give the name of the interaction. R₁ cysteine tyrosine threonine arginine R₂ cysteine phenylalanine glutamine aspartate specific interaction? OO yes O yes O no no OO O yes no yes no name of specific interaction 0 П 0 0Question 14 The folding of an unfolded protein proceeds from low entropy disordered state to a single high entropy, low energy native conformation O True O False Question 15 The GroES subunit has 14 identical 549-residue subunits arranged in two stacked rings with 7 subunits eac True False
- Question 9 Choose the CORRECT statement. O A polypeptide chain may have abrupt changes in direction and restriction in geometry because of the presence of glycine O A polypeptide chain may have abrupt changes in direction and restriction in geometry because of the presence of valine O A polypeptide chain may have abrupt changes in direction and restriction in geometry because of the presence of arginine O A polypeptide chain may have abrupt changes in direction and restriction in geometry because of the presence of prolineQUESTION 20 A helices and ß sheets are examples of protein structure. secondary structure Primary Structure quaternary structure tertiary structure QUESTION 21 Which of the following describes an enzyme with only the amino acids present, without any metal ions or vitami that might be needed for catalysis? Apoenzyme O Enzyme Coenzyme O Haloenzyme 78 Mostly cloudy Click Save and Submit to save and submit. Click Save All Answers to save all ansuers.Question 4. If you were to synthesize a tetrapeptide consisting of all alanine residues, you would have how many bonds between carbon and nitrogen?