4. Below is data obtained for an unknown protein's dihedral angles. Each dot representsthe dihedral angles of each amino acid.i.psiii.18012060C-60-1200.00050.020.02--1880 -120What secondary structure(s) are present in the unknown protein?-60phi601200.0005Why is there a lot of white space?180

4. Below is data obtained for an unknown protein's dihedral angles. Each dot represents the dihedral angles of each amino acid. i. psi ii. 180 120 60 O -60 -120 -180 -180 002 -120 002- -60 phi .CO 60 120 180 What secondary structure(s) are present in the unknown protein? Why is there a lot of white space?

4. Below is data obtained for an unknown protein's dihedral angles. Each dot represents the dihedral angles of each amino acid. i. psi ii. 180 120 60 O -60 -120 -180 -180 002 -120 002- -60 phi .CO 60 120 180 What secondary structure(s) are present in the unknown protein? Why is there a lot of white space?

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

What is the monomer of a nucleic acid macromolecule?
The monomers that make up proteins are called _____ a. nucleotides b. disaccharides c. amino acids d. chaperones
7/ Hemoglobin is an example of a protein with A. Primary structure only. B. two protein chains held together. C. a quaternary structure. D. primarily a B-pleated sheet structure.
7. Native conformation of proteins may result from: a) hydrophobic interactions b) H-bonds c) ionic bonds d) covalent bonds e) all a-d may contribute to native conformation
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.
3. Why do we need to study the four levels of protein structure? Cite its practical use to our day-to-day life.
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.
6.All of the following types of interactions cooperate in stabilizing the tertiary structures of globular proteins except____. a.Disulphide bond b.Hydrogen bond c.Ionic interactions d.Peptide bond
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.
2- ‏Some proteins contain additional amino acids that arise by modification of an amino acid already present in a peptide , examples include: a) Gamma Amino Butyric Acid. b) 5 - hydroxy Lysine c) 4 - hydroxy proline d) All of the above e) None of the above
1. Describe how each of the following relates to protein configuration: primary structure - secondary structure - tertiary structure - quaternary structure -
1. Which best describes the contribution of primary (1’) structure of polypeptides to the native conformation of proteins: a) Structure that results from intrachain interactions of amino acid side chains b) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence of amino acids from beginning to end of molecule.