2. Evaluate the secondary structure of proteins. Which of the following differentiates alpha structures to those beta structures? ? A. alpha structures are helices and beta structures are pleated sheets B. alpha structures are primary and beta structures are secondary C. alpha structures are parallel and beta structures are antiparallel D. alpha structures are L and beta structures are D

2. Evaluate the secondary structure of proteins. Which of the following differentiates alpha structures to those beta structures? ? A. alpha structures are helices and beta structures are pleated sheets B. alpha structures are primary and beta structures are secondary C. alpha structures are parallel and beta structures are antiparallel D. alpha structures are L and beta structures are D

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...

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Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternary
4. Alpha helices, loops, and beta sheets are examples of protein secondary structure. Beta sheets can be parallel or anti-parallel. Identify all hydrogen bonds (four) in the two example sheets below. Identify which is the parallel and which is the anti-parallel. C-term Cterm H. C-term N term H. parallel anti-parallel parallel anti-parallel
2. a. In the following diagram of a portion of a protein, label the types of interactions that are shown. b. What level of protein structure are these interactions producing? b. CH CH3 CH3 Polypeptide backbone CH2 H3C H3Ç 10 CH С—ОН - CH,-S-S-CH,- а. CH2 с. -CH,-CH,-CH2-CH2-NH 0-C-CH2- d.
3. The figure below depicts a protein folding into its final shape. If this was a cytoplasmic protein: goa oog ge Tertiary Structure a. The chemical properties of the amino acids in black are likely (circle): Polar or Nonpolar Primary Structure b. The chemical properties of the amino acids in white are likely (circle): Polar or Nonpolar
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2. What is the secondary structure of protein? A. The oligomer protein B. Local conformation of the parts of polypeptide chain C. The combination of the protomers D. Two polypeptide chains making the helix E. The sequence of amino acid residues O
The function of a protein depends on ... . and the 3D shape of a protein is controlled by Select one: ut of O a. Its ability to recognize certain substances, Primary structure O b. Its ability to resist temperature, Secondary structure uestion c. Its ability to resist pH, Quaternary structure O d. Its ability to recognize specific substances, Tertiary structure O e. Its ability to bind to many molecules, Secondary structure
4. Tertiary structure of a protein describes: A. Sequence of amino acids B. Location of disulphide bonds C. Amino terminal end amino acid D. The nature of protein folding 5. Study of linear sequence of amino acids is done by all techniques listed except: A. End group analysis B. Hydrolysis by proteolytic enzymes C. Analyzing the content of each aminOacid D. Denaturing the protein 6. Primary structure decides: A. Rate of synthesis of protein B. Biological activity of the protein C. Rate of degradation of the protein D. Effect of proteolytic enzymes on protein
Indicate the level(s) of protein structure to which each of thefollowing contributes:a. amino acid sequenceb. b-pleated sheetc. hydrogen bondd. disulfide bond
4. Explain and draw a representative picture of the four levels of protein structure. How are they defined and what bonds keep them together? ? What effect does the a
II. Differentiate the following in terms of proteins' structural features in living systems. 1. primary structure vs quaternary structure 2. H-bonding vs disulfide linkage
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.