Which of the following types of bonds are responsible for the secondary structures of proteins? Covalent bond dislufide linkages Hydrogen bonds 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 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 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 environment
- Question 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 1Predicting Secondary Structure Which of the following peptides is more likely to take up an -helical structure, and why? (a) LKAENDEAARAMSEA (b) CRAGGFPWDQPGTSNQUESTION 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 a
- 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 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 0 016:51 Pictured here is the antibiotic daptomycin: H3N H EO HN HOOC CONH2. ONH HOOC NH но. NH COOH H NH2 HOO How many of the amino acid Q are there in this structure? Your answer is just a number. Ex 0, 1, 2, 3
- 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)5 pts Question 9 95 58 40 HS HS SH 65 8 M urea and 72 B-mercaptoethanol 65 Hs84 Hs- SH 72 26 HS 110 SH 84 26 110 95 124 40 58 Native ribonuclease Denatured reduced ribonuclease Figure 2.53 Biochemistry, Seventh Edition O 2012 W. H. Freeman and Company The image above shows how Anfinsen unfolded ribonuclease for his classic experiment to see if proteins contain all necessary information for adopting their folded states on their own. To achieve proper refolding and ribonuclease activity, Anfinsen must have: trick question: ribonuclease cannot adopt its folded state without the help of cellular machinery removed the mercaptoethanol followed by the urea very carefully removed both the urea and mercaptoethanol at the same time removed the urea followed by the mercaptoethanolQuestion 4. If you were to synthesize a tetrapeptide consisting of all alanine residues, you would have how many bonds between carbon and nitrogen?