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.

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.

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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8) The figure shows an unfolded polypeptide consisting of six amino acids. Describe how cooperativity will drive protein folding of the polypeptide chain into an alpha-helixe- 10EEHOW is AG changed as each amino acid is incorporated into the secondary structure - s)? O H O H 3 H. H. 5 CH-C H. 6 -N-CH-C- OH O H,N CH-C -N CH C-N CH CH CH2 CH2 CH2 CH2 CH OH CH H;C CH3
What type of IPF would you expect from the following R groups in a tertiary structure of a protein? Glutamic acid and Lysine Show answer choices lon-dipole attraction Hydrogen bond attraction London dispersion forces Disulfide bond Salt bridge (ion-ion attraction) Question 34 What type of IPF would you expect from the following R groups in a tertiary structure of a protein? Serine and Aspartic acid Show answer choices Hydrogen bond attraction Blon-dipole attraction Salt bridge (ion-ion attraction) London dispersion forces D E Disulfide bond 0/3
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-100 100 8. This is a helical wheel projection. The following amino acids of your protein were predicted to participate in an alpha helix: DRMVEHACKSI. a. Plot these amino acids in the helical wheel projection below. b. Is the alpha helix in your protein hydrophobic, amphipathic or hydrophobic? c. Would you expect this helix to be on the interior of the protein, exposed, or partially exposed?
TERTIARY STRUCTURE (A) (B) (C) Fg Eet Galand Sen 20e Figure 6. Examples of the arrangement of a-helices and B-sheets in folded protein domains. Copyright 2013 from Essential Cell Biology, 4th Edition by Alberts et al. Reproduced by permission of Garland Science/ Taylor & Francis LLC. Figure 6 shows three examples of how secondary structure elements can be arranged in relation to one another in the functional, folded form of a complete protein or one compact portion of a protein. The overall three-dimensional shape (or conformation) of a protein is its tertiary structure. • What do you think holds together the various secondary structural elements in a particular three-dimensional pattern? (Hint: Look back at Figure 5 - what is sticking out from the sides of the a-helices and B-strands?)
Tertiary structures refer to the three-dimensional arrangement of every atom in the molecule. On the other hand, primary structures refer to the stable arrangements of amino acid residues in a protein that give rise to recurring patterns. O Both statements are correct O Both statements are incorrect O The first statement is incorrect while the second statement is correct O The first statement is correct while the second statement is incorrect
Based on your understanding of the principles guiding folding of globular protein, briefly explain why a folded protein cannot consist of a single alpha-helix or single beta-strand
3. Amino Acid Sequence and Protein 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. 1 3 5 6 7 8 9 10 Ile - Ala - His - Thr - Tyr - Gly - Pro - Phe-Glu – Ala- - 11 12 13 14 15 17 20 Ala - Mat - Cys- Lys - Trp - Glu-Ala-Gln-Pro - Asp- 16 18 19 21 22 23 24 25 26 27 28 Gly - Met-Glu - Cys - Ala - Phe - His - Arg (a) Where might bends or ß 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, lle, Thr, Ala, Gln, Lys. Explain your reasoning.
can you please check if my answers are correct
Beta ( ? ) sheets are a type of secondary structure in proteins. A segment of a single chain in an antiparallel ? sheet has a length of 80.5 Å . How many residues are in this segment?
Helices can be described by the notation nm,where n is the number of residues per helical turn and m is the number of atoms, including H, in the ring that is closed by the hydrogen bond. Would a 310 helix be more or less steep than an α helix? why?
β-pleated sheets and α-helices arise more from interactions in the peptide backbone than from the “R” groups of the individual monomers; they are examples of the (????) structure of a protein. Primary Tertiary Secondary Quaternary (????) are comprised of a nitrogenous base, a pentose sugar, and a phosphate group. Monosaccharides Amino acids Proteins Nucleotides (????) is the RNA transcript of the DNA sequence that determines the primary structure of a protein. mRNA lncRNA tRNA rRNA If a substance such as a lipid isn’t soluble in water it might be described as (????) Hydrophilic Hydrophobic