Answer just #2 1. Determine whether each of the following statements describes the primary,secondary, tertiary, or quaternary stucture of a protein.а.Peptide bonds join amino acids in a polypeptide chain.b.Two polypeptide chains are held together by hydrogen bonds.c.Hydrogen bonds form between adjacent segments of the backbone of thesame protein to form a "folded fan" structure.2. List the type of denaturing agent described by the following treatments:a. disrupting the disulfide bonds in hair to straighten itb. baking the proteins in dough to make bread

1.a peptide bond is the back bone of the protein chain. It is the amide linkage in which COOH of one…

1. Determine whether each of the following statements describes the primary, secondary, tertiary, or quaternary stucture of a protein. а. Peptide bonds join amino acids in a polypeptide chain. b. Two polypeptide chains are held together by hydrogen bonds. С. Hydrogen bonds form between adjacent segments of the backbone of the same protein to form a "folded fan" structure. 2. List the type of denaturing agent described by the following treatments: a. disrupting the disulfide bonds in hair to straighten it b. baking the proteins in dough to make bread

1. Determine whether each of the following statements describes the primary, secondary, tertiary, or quaternary stucture of a protein. а. Peptide bonds join amino acids in a polypeptide chain. b. Two polypeptide chains are held together by hydrogen bonds. С. Hydrogen bonds form between adjacent segments of the backbone of the same protein to form a "folded fan" structure. 2. List the type of denaturing agent described by the following treatments: a. disrupting the disulfide bonds in hair to straighten it b. baking the proteins in dough to make bread

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter3: Biological Molecules: The Carbon Compounds Of Life

Section: Chapter Questions

Problem 8TYK: The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices...

See similar textbooks

Similar questions

1. What are the effects of a) amino acid composition and sequence and b) intramolecular and intermolecular forces of attraction to protein folding? 2. What molecular property of amino acids can be used to justity the concept that the "molecular part of the protein can exhibit the same property as the molecular 'whole' (protein molecule?). Provide a comprehensive discussion using one molecular property. 3. Discuss two metabolic disorders which are caused by protein misfolding. Explain the metabolic consequence of the disorder. 4. If a non-science person asks you what protein folding is and how the concept is related to metabolic disorders, how are you going to explain the concept? (please summarize the concepts used, thank you!)
1.Describe in detail how to detect the primary structure of protein. 2.Given a mixture of lysine,histidine and cysteine.The isoelectronic point of the amino acids are as follows: histidine:7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.
5 (a) Describe in detail how you will determine the primary structure of protein. You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows: Histidine 7.64 Lysine 9.74 Cystenie 5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.
1.Describe in detail how to determine the primary structure of protein. 2.You have been given a mixture of lysine, histidine and cysteine.The isoelectric point of the amino acids are as follows; histidine 7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.
1.a.If this molecule was the side chain of an amino acid, in a protein, what tertiary structure stabilizers could be present? b.Make a key and use color to highlight what part of you structure can be stabilized in each manner?
SDS-PAGE gels are used to study changes in protein primary structure. Which of the following statements about SDS-PAGE gels is correct? A. The negatively charged proteins will move towards the negatively charged electrode in the SDS-Page chamber B. A detergent is needed to disrupt protein secondary, tertiary, and quaternary structure before a gel can be run C. No "stains" or other treatments are needed to "see" the protein bands on a gel D. Long polypeptides move a further distance from the loading well in a SDS-PAGE gel than short polypeptides
1. Explain how each primary structure of a protein affects its properties and how denaturation changes the structure. 2. Explain how each secondary structure of a protein affects its properties and how denaturation changes the structure.
Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data. Consider the following amino acid sequence.(a) Where might bends or β turns occur?(b) Where might intrachain disulfide cross-linkages be formed?(c) Assuming that this sequence is part of a larger globular protein, indicate the probable location (external surface or interior of the protein) of the following amino acid residues: Asp, Ile, Thr, Ala, Gln, Lys. Explain your reasoning.
Our understanding of how proteins fold allows us to make predictions about protein structure based on primary amino acid sequence data. Consider the following amino acid sequence :a)Where might bends or βturns occur? b)Where might intrachain disulphide cross-linkages be formed? c)Assuming that this sequence is part of a bigger globular protein, indicate the probable location (on the surface or interior of the protein) of the following amino acid residues: Asp, Ile, Thr, Ala, Gln and Lys. Explain your reasoning
The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices unwind. c. sheet structures unfold. d. tertiary structure is changed. e. quaternary structures disassemble.
A protein in its native three dimensional conformation is cleaved with trypsin. According to the amino acid sequence, there are 9 residues where trypsin could cleave, yet only 3 fragments were produced from the digest. What conclusion can be made about protein structure that would lead to this result? The protein has multiple domains b. The protein is highly compacted, minimally accessible by solvent molecules c. The protein has quaternary structure d. The protein has a dynamic structure, highly accessible by solvent molecules e. The protein is compromised only of alpha helices
1) Explain the meanings of the "Motif" and "Domain" in the structuralhierarchy of proteins. Which structural groups can domains beclassified into? Give examples of and illustrate with diagrams at least4 simple protein motifs. 2) Explain the meaning of protein family, superfamily and fold. How dothese reflect structural and evolutionary relatedness?