Imagine the main chain of a protein bends back on itself, so that two amino acid residues R₁ and R₂ come close to each other.In the table below are four possibilities for what R₁ and R2 might be. In each case, decide whether a specific interaction could form between theresidues. If a specific interaction could form, give the name of the interaction.R₁R₂specificinteraction?name of specificinteractionxyesalaninevalineO noisoleucineasparagine○ yesO noyeslysineglutamate☐O noyesthreonineasparagineO no

Sure, let's delve into each interaction:1. Valine - Alanine (Hydrophobic Interaction): Both valine…

Answered: Imagine the main chain of a protein…

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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Researchers discover a new amino acid. Its R-group exclusively has hydrogen and carbon atoms. What behavior will this amino acid show? O Relative to the amino acids found in organisms, its interactions with water will be very high. It is hydrophilic. Relative to the amino acids found in organisms, its interactions with water will be intermediate. It is hydrophobic.
The amino acid histidine has ionizable groups with pK, values of 1.8, 6.0, and 9.2, as shown. COOH H₂N-CH CH, H pH = 1.29 COO H₂N-CH 1.8 CH pk, lonizable -COOH-COO- group Incorrect CH, H COO H₂N-CH 6.0 CH pk, CH, H H N CH -HisH¹-His COO H₂N-CH NH - NH, A biochemist makes up 85 mL of a 0.10 M solution of histidine at a pH of 5.5. She then adds 60 mL of 0.10 M HCI. What is the pH of the resulting solution? CH, H 9.2 C pk CH Macmillan Iraming T im be the [His IM.
Identify the part of a generic amino acid that reacts with base and the part that reacts with acid. Briefly explain your answer.Hint: Draw Lewis structures for ammonia (NH 3) and acetic acid (CH 3COOH).
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
Highlight each peptide bond in the molecule below. In addition, list the common names of the smaller molecules that would be released if all the peptide bonds were hydrolyzed. You can add more rows to the table if you need to. (Note: you do not need to list water.) If there are no peptide bonds in the molecule, just check the no peptide bonds box below the drawing area. Ono peptide bonds Add Row I Don't Know H₂N-C Submit CH₂ CH C–NH–CH—CO0 CH, CH3 molecules released if peptide bonds hydrolyzed (list one name per row) 0 CH3 00 X S X 3 alo Ar © 2023 McGraw Hill LLC. All Rights Reserved. Terms of Use | Privacy Center Accessibility
Identify the features of the two bonded amino acids depicted in the image. HOHH | || | | N-C-C-N-C-C CH CH₂2 CH₂2 CH₂ CH₂ I I CH₂ CH₂ NH₂+ O OH Answer Bank hydrophilic side chain hydrophobic side chain peptide bond carboxyl group amino group
Bovine chymotrypsinogen has a molecular weight of 25.6 kDa. Amino acid analysis shows that this enzyme is 9% alanine (Mr 89.1). Calculate how many alanine residues are present in a molecule of bovine chymotrypsinogen. Round your answer to the nearest whole number.
i 3. Identify which of the following pairs of amino acid residues can have London dispersion forces between their side chains. a. Alanine and Glycine b. Leucine and Isoleucine Valine and Asparagine C. d. Threonine and Tyrosine
All amino acids have two ionizable functional groups: an α‑amino group (average pKa of 9.4) and an α‑carboxylic acid group (average pKa of 2.2). Aspartic acid has an ionizable side chain (R group) with a pKa of about 3.8. One of the possible ionization states of aspartic acid is shown in the image. At what pH would the structure be the predominant ionization state? Consider the ionization state of all three of the functional groups.
Which statement is false about a globular protein that performs its biological function as a single independent polypeptide chain? O a. Its tertiary structure is likely stabilized by the interactions of amino acid side chains in non-neighboring regions of the polypeptide chain. It likely has extensive quaternary structure to maintain its globular shape. b. Oc. Non-covalent forces are the primary source of stability for the secondary and tertiary structure. Ⓒd. it could contain a-helices that are stabilized by hydrogen bonding.
Proteins 1 and 2 interact strongly. A significant part of the interaction is between the amino acid side chains shown below. Protein 1= arginine C6H14N402 . Protein 2 = glutamic acid C5H9NO4 A mutation occurs in protein 2 that changes the amino acid shown above to one of the amino acids shown below. What change should disrupt the interaction between proteins 1 and 2 the most? the least? Protein 2- aspartic acid C4H7NO4, protein 2= Lysine C6H14N20 Protein 2= serine C3H7NO3 and protein 2= leucine C6H13NO2 aspartic acid would be the most and leucine would be the least aspartic acid would be the most and serine would be the least lysine would be the most and serine would be the least lysine would be the most and aspartic acid would be the least
Q1. Would an amino acid with the given side chain be most likely to be found in the hydrophobic or hydrophilic region of a protein? Circle one below. A. B. C. -CH₂-CH-CH3 I CH3 O -CH2-C-NH2 -CH-CH3 | ОН Circle one: Hydrophilic region // Hydrophobic region Circle one: Hydrophilic region // Hydrophobic region Circle one: Hydrophilic region // Hydrophobic region

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