Which statement is true regarding denaturation process? Question 21 options: Protein experiences hydrolysis as it denatures and alters its structure. Denaturation is the process of altering the shape of a protein that involves breaking the amide bonds. Denaturation is the process of altering the shape of a protein without breaking the amide bonds. As protein denatures, new peptide bonds form with the added amino acids

Which statement is true regarding denaturation process? Question 21 options: Protein experiences hydrolysis as it denatures and alters its structure. Denaturation is the process of altering the shape of a protein that involves breaking the amide bonds. Denaturation is the process of altering the shape of a protein without breaking the amide bonds. As protein denatures, new peptide bonds form with the added amino acids

Anatomy & Physiology

1st Edition

ISBN:9781938168130

Author:Kelly A. Young, James A. Wise, Peter DeSaix, Dean H. Kruse, Brandon Poe, Eddie Johnson, Jody E. Johnson, Oksana Korol, J. Gordon Betts, Mark Womble

Publisher:Kelly A. Young, James A. Wise, Peter DeSaix, Dean H. Kruse, Brandon Poe, Eddie Johnson, Jody E. Johnson, Oksana Korol, J. Gordon Betts, Mark Womble

Chapter2: The Chemical Level Of Organization

Section: Chapter Questions

Problem 27RQ: Which of the following is a functional group that is part of a building block of proteins? phosphate...

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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 proline
QUESTION 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 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)
Please Answer numbers 1, 2 & 3 thank you 1. Which of the following intermolecular molecular forces of attraction is disrupted when a native protein is added with acetic acid? a. Hydrogen bond b. Peptide bond c. Disulfide bond d. Salt bridge e. van der Waals force 2. Suppose a protein sample with a fragment containing the following amino acid sequence is subjected to various chemical assay/tests. - Ala-Gly-Phe-Met-Cys- which of the following test will the sample be positive? a. Lead-sulfide test b. Hopkins cole's test c. Millon's test d. Xanthoproteic test 3. Suppose a protein sample with a fragment containing the following amino acid sequence is subjected to various chemical assay/tests. - Ala-Gly-Trp-Phe-Met-Cys- What is observed when the protein sample is subjected to Millon’s test? a. Violet interface b. Red precipitate/solution c. Brown/black precipitate d. Yelllow product e. No observable result
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.
A protein that is normally found in an aqueous solution has these amino acids in its primary structure: glutamic acid, lysine, leucine, arginine, and tryptophan. Predict the location of each amino acid: in the interior portion of the protein (away from water) or on the outside of the protein (facing water). glutamic acid _________________________ lysine _________________________ leucine _________________________ arginine ________________________ tryptophan _________________________ Indicate whether each of the following statements describes a reversible competitive inhibitor, reversible noncompetitive inhibition, or an irreversible inhibitor. ________ a. It bonds covalently to the active site ________ b. The inhibitor effect can be reversed by the addition of more substrate ________ c. Inhibitor structure resembles that of the substrate ________ d. The inhibitor and substrate cannot bind to the enzyme simultaneously.
A protein that is normally found in an aqueous solution has these amino acids in its primary structure: glutamic acid, lysine, leucine, arginine, and tryptophan. Predict the location of each amino acid: in the interior portion of the protein (away from water) or on the outside of the protein (facing water). glutamic acid _________________________ lysine _________________________ leucine _________________________ arginine ________________________ tryptophan _________________________
Intrinsically disordered proteins may: Question 39 options: lack a hydrophobic core. All of the answers are correct. wrap around their targets. have multiple interaction partners.
GABA (B) Need help answering these questions about the GABA(B) protein.  What class (globular, fibrous, membrane) protein is the protein Identify the organism (or organisms that have this protein) Identify the cellular location of this protein Describe the function Find the primary structure (list it on a slide) Describe secondary structure (alpha-helix, beta sheet, and how many of each and what percent of the total protein) Find a picture of the tertiary structure (which should also show secondary structure) Does the protein have a quaternary structure, if so what is it?

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	Protein experiences hydrolysis as it denatures and alters its structure.
	Denaturation is the process of altering the shape of a protein that involves breaking the amide bonds.
	Denaturation is the process of altering the shape of a protein without breaking the amide bonds.
	As protein denatures, new peptide bonds form with the added amino acids.