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Cyw Ala Ατα Ile Ausn Lou Asp aly Lys Ser Which molecule below is asubunit of...
t How are donaturation and varovalo airterent a. Rydrolysis resulte to the formation of water. Hydrolysis...
t How are donaturation and varovalo airterent a. Rydrolysis resulte to the formation of water. Hydrolysis only takes place in the cytopa c. Hydrolysis results in breakingole d. Hydrolysis results in breaking ovalent bo How is folding related to function? • Folding and function are not related.. Proper folding results in propertune 0. Proper folding results in reduced un roper folding results in arratiefunct Molecules that a t folding are called a. Foldons which cellular environment is . Cytoplasm c....
10. The peptide shown has the amino acid sequence: A. Val-Ser-Ile-Glu-Lys B. Lys-Glu-Ile-Ser-Val C. Thr-Asp-Leu-Gln-Arg D....
10. The peptide shown has the amino acid sequence: A. Val-Ser-Ile-Glu-Lys B. Lys-Glu-Ile-Ser-Val C. Thr-Asp-Leu-Gln-Arg D. Val-Asp-Ile-Glu-Arg 11. Which of the following describes the entire three- dimensional structure of a single polypeptide? A. Secondary structure B. Quaternary structure C. Tertiary structure D. Primary structure 12. What is the primary driving force in the formation of protein tertiary structure? A. Energy released when additional ion pairs are formed. B. The exclusion of non-polar substances from aqueous solution. C. The formation of...
The _______ of amino acids in a protein is referred to as its primary structure
24. The _______ of amino acids in a protein is referred to as its primary structure. A) twisting B) sequencing C) folding D) none of these 25. The structure of a protein is most important because the _______ of the amino acids determines its overall shape, function and properties. A) primary, twisting B) primary, sequencing C) secondary, twisting D) secondary, folding E) none of these 26. The secondary structure of a protein is due to_______ between amino acid residues. A) hydrophobic interactions B) hydrogen bonding...
Which of the following is true of secondary structure in protein folding? Pick ALL that apply....
Which of the following is true of secondary structure in protein folding? Pick ALL that apply. A. It involves hydrogen bonding. B. It involves the side chains. C. It involves hydrophobic interactions. D. It results in alpha helicies with the side chains hidden inside the helix. E. It results in beta-pleated sheets with side chains sticking out of the plain of the sheet. F. It involves the peptide backbone.
5. Which of the following molecules form complex structures linked by covalent bonds through Lys, HyLys,...
5. Which of the following molecules form complex structures linked by covalent bonds through Lys, HyLys, or His residues? A) Collagen B) Alpha keratin C) Hemoglobin D) Myoglobin E) Beta barrels 6. Which of the following correlates to the classic experiment demonstrating that reduced and denatured RNase A could refold into the native form? A) Disulfide bonds do not stabilize folded proteins B) Reducing agents denature proteins C) 1° structure can determine 3° structure D) Urea cleaves disulfide bonds E)...
Complete hydrolysis of an unknown basic decapeptide gives Gly, Ala, Leu, Ile, Phe, Tyr, Glu, Arg,...
Complete hydrolysis of an unknown basic decapeptide gives Gly,
Ala, Leu, Ile, Phe, Tyr, Glu, Arg, Lys, and Ser.
Problem 24-44 ConstantsI Periodic Table Complete hydrolysis of an unknown basic decapeptide gives Gly, Ala, Leu, lle, Phe, Tyr, Glu, Arg, Lys, and Ser. Terminal residue analysis shows that the N terminus is Ala and the C terminus is lle. Incubation of the decapeptide with chymotrypsin gives two tripeptides, A and B, and a tetrapeptide, C. Amino acid analysis shows that...
Which one of the following represents a tetrapeptide? A) Val-Ile-Asp-Asp B) Ala-Ala-Ala-Ala-Val-Val C) Ala-Ser-Val-Val-Ile D) Ser-Ser-Ala-Ala-Gly-Gly-Glu-Glu...
Which one of the following represents a tetrapeptide? A) Val-Ile-Asp-Asp B) Ala-Ala-Ala-Ala-Val-Val C) Ala-Ser-Val-Val-Ile D) Ser-Ser-Ala-Ala-Gly-Gly-Glu-Glu E) Ser-Ala-Thr-Pro-Leu In the octapeptide, Cys-Ile-Ser-Asp-Gly-His-Gly-Gly, which is the N-terminal amino acid A) Ser B) Ile C) Asp D) Cys E) Gly If an amino acid has one carboxyl group and one amino group, and the pka's are 2.4 and 9.8 respectively, what is its isoelectric point? A) 3.7 B) 6.1 C) 7.0 D) 7.9 E) 12.2 Which of the following will migrate toward...
1) Select all that apply. Globular proteins: a)are found in hair and wool. b)include myoglobin and...
1) Select all that apply. Globular proteins: a)are found in hair and wool. b)include myoglobin and collagen. c)are usually water soluble. d)aggregate in aqueous media. e)are often made of β-pleated sheet and α-helix sections wrapped into compact structures. 2) Select all that apply. The Bohr effect: a)depends on the atomic orbital structure of hydrogen. b)can be summarized as a reduction in the oxygen affinity of hemoglobin with decreasing pH. c)is explained by the protonation of key amino acids, including the...
What fragments will be obtained by a trypsin hydrolysis of the following octapeptide? Ala-Val-Trp-Lys-Phe-Gly-Arg-Met A) Ala-Val-Trp-Lys-Phe...
What fragments will be obtained by a trypsin hydrolysis of the following octapeptide? Ala-Val-Trp-Lys-Phe-Gly-Arg-Met A) Ala-Val-Trp-Lys-Phe and Gly-Arg-Met 3) Ala-Val-Trp-Lys-Phe-Gly and Arg-Met - Ala-Val-Trp-Lys and Phe-Gly-Arg and Met ) Ala-Val-Trp-Lys and Phe and Gly-Arg and Met ) Ala-Val-Trp and Lys-Phe-Gly and Arg-Met Bradykinin is a nonapeptide, Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg. In addition to one mole of Arg, what peptides are present after hydrolysis of bradykinin with chymotrypsin? A) Arg-Pro-Pro and Gly-Phe and Ser-Pro-Phe B) Pro-Pro-Gly and Phe-Ser-Pro-Phe-Arg C) Arg-Pro-Pro-Gly-Phe and Ser-Pro-Phe ?) Arg-Pro-Pro-Gly-Phe-Ser...
19) The form of dipeptide aspatylserine (Asp-Ser) obtained from two amino acids, aspartic acid an...
19) The form of dipeptide aspatylserine (Asp-Ser) obtained from two amino acids, aspartic acid and serine, whose structures are shown here, is HiN-CH-C-0HIN-CH-C-0 CH2 CH OH aspartic acid serine A HN-CH-C-o-N-CH-C-o CH OH CH2 coo -(H-C-o-H-c-o CH OH CH2 HIN CH-C-N-CH-C-O CH OH CH H-CH-CH CH CH OH coo- 20) Where is the peptide bond located in this dipeptide? serine valine a) the CO-NH joining serine and the valine b) the doubly bonded oxygen just left of center between the...
t How are donaturation and varovalo airterent a. Rydrolysis resulte to the formation of water. Hydrolysis only takes place in the cytopa c. Hydrolysis results in breakingole d. Hydrolysis results in breaking ovalent bo How is folding related to function? • Folding and function are not related.. Proper folding results in propertune 0. Proper folding results in reduced un roper folding results in arratiefunct Molecules that a t folding are called a. Foldons which cellular environment is . Cytoplasm c....
10. The peptide shown has the amino acid sequence: A. Val-Ser-Ile-Glu-Lys B. Lys-Glu-Ile-Ser-Val C. Thr-Asp-Leu-Gln-Arg D. Val-Asp-Ile-Glu-Arg 11. Which of the following describes the entire three- dimensional structure of a single polypeptide? A. Secondary structure B. Quaternary structure C. Tertiary structure D. Primary structure 12. What is the primary driving force in the formation of protein tertiary structure? A. Energy released when additional ion pairs are formed. B. The exclusion of non-polar substances from aqueous solution. C. The formation of...
5. Which of the following molecules form complex structures linked by covalent bonds through Lys, HyLys, or His residues? A) Collagen B) Alpha keratin C) Hemoglobin D) Myoglobin E) Beta barrels 6. Which of the following correlates to the classic experiment demonstrating that reduced and denatured RNase A could refold into the native form? A) Disulfide bonds do not stabilize folded proteins B) Reducing agents denature proteins C) 1° structure can determine 3° structure D) Urea cleaves disulfide bonds E)...
Complete hydrolysis of an unknown basic decapeptide gives Gly,
Ala, Leu, Ile, Phe, Tyr, Glu, Arg, Lys, and Ser.
Problem 24-44 ConstantsI Periodic Table Complete hydrolysis of an unknown basic decapeptide gives Gly, Ala, Leu, lle, Phe, Tyr, Glu, Arg, Lys, and Ser. Terminal residue analysis shows that the N terminus is Ala and the C terminus is lle. Incubation of the decapeptide with chymotrypsin gives two tripeptides, A and B, and a tetrapeptide, C. Amino acid analysis shows that...
Which one of the following represents a tetrapeptide? A) Val-Ile-Asp-Asp B) Ala-Ala-Ala-Ala-Val-Val C) Ala-Ser-Val-Val-Ile D) Ser-Ser-Ala-Ala-Gly-Gly-Glu-Glu E) Ser-Ala-Thr-Pro-Leu In the octapeptide, Cys-Ile-Ser-Asp-Gly-His-Gly-Gly, which is the N-terminal amino acid A) Ser B) Ile C) Asp D) Cys E) Gly If an amino acid has one carboxyl group and one amino group, and the pka's are 2.4 and 9.8 respectively, what is its isoelectric point? A) 3.7 B) 6.1 C) 7.0 D) 7.9 E) 12.2 Which of the following will migrate toward...
What fragments will be obtained by a trypsin hydrolysis of the following octapeptide? Ala-Val-Trp-Lys-Phe-Gly-Arg-Met A) Ala-Val-Trp-Lys-Phe and Gly-Arg-Met 3) Ala-Val-Trp-Lys-Phe-Gly and Arg-Met - Ala-Val-Trp-Lys and Phe-Gly-Arg and Met ) Ala-Val-Trp-Lys and Phe and Gly-Arg and Met ) Ala-Val-Trp and Lys-Phe-Gly and Arg-Met Bradykinin is a nonapeptide, Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg. In addition to one mole of Arg, what peptides are present after hydrolysis of bradykinin with chymotrypsin? A) Arg-Pro-Pro and Gly-Phe and Ser-Pro-Phe B) Pro-Pro-Gly and Phe-Ser-Pro-Phe-Arg C) Arg-Pro-Pro-Gly-Phe and Ser-Pro-Phe ?) Arg-Pro-Pro-Gly-Phe-Ser...
19) The form of dipeptide aspatylserine (Asp-Ser) obtained from two amino acids, aspartic acid and serine, whose structures are shown here, is HiN-CH-C-0HIN-CH-C-0 CH2 CH OH aspartic acid serine A HN-CH-C-o-N-CH-C-o CH OH CH2 coo -(H-C-o-H-c-o CH OH CH2 HIN CH-C-N-CH-C-O CH OH CH H-CH-CH CH CH OH coo- 20) Where is the peptide bond located in this dipeptide? serine valine a) the CO-NH joining serine and the valine b) the doubly bonded oxygen just left of center between the...
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