identifying specific interactions between residues in a protein www-awu.aleks.com 00 Imagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R, come close to each other. Here's what R looks like: CH- CH₂ CH₂ 0=0 NH₂ O yes X Could R, form a disulfide bond with R₂ at physiological pH, if R2 were the right kind of residue? O no If you said R, could form a disulfide bond with R₂, what would R₂ have to be? If there's only one possibility, write its 3-letter code. If there is more than one possibility, write the 3-letter code of any of them. Explanation Check PH LLC. All Rights Reserved Terms of Use Privacy Center 1 Accense

identifying specific interactions between residues in a protein www-awu.aleks.com 00 Imagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R, come close to each other. Here's what R looks like: CH- CH₂ CH₂ 0=0 NH₂ O yes X Could R, form a disulfide bond with R₂ at physiological pH, if R2 were the right kind of residue? O no If you said R, could form a disulfide bond with R₂, what would R₂ have to be? If there's only one possibility, write its 3-letter code. If there is more than one possibility, write the 3-letter code of any of them. Explanation Check PH LLC. All Rights Reserved Terms of Use Privacy Center 1 Accense

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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The amino acid histidine has ionizable groups with pKą values of 1.8, 6.0, and 9.2, as shown. COOH T H₂N-CH | CH₂ H -O pH UT = ZI Ionizable -COOH group CH H₂N-CH T 1.8 COO- pk₁ CH2 UI COO™ H IZ CH -HisH+ COO™ + H₂N-CH 6.0 pK₂ CH ₂ UI -His H CH -NH COO™ H₂N-CH 9.2 pk3 CH ₂ UI —NH₂ H A biochemist makes up 80 mL of a 0.11 M solution of histidine at a pH of 5.1. She then adds 60 mL of 0.10 M HCl. What is the pH of the resulting solution? CH
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Draw the structure of the peptide WAKEP. Write the full name of each amino acid above the relevant R-group. Mark all of the peptide bonds on your drawing. Mark the charged groups on your drawing. Assuming that pH = 7, what is the Net Charge for the peptide? Type your numeric answer and submit -7 X You are incorrect
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.
10. Use the information in the table below to draw the structure of the predominant form of each amino acid at physiological pH (pH = 7.4) R side chain pKa (a-COOH) -CH₂CH(CH3)2 -(CH2)4NH2 -(CH2)2CO2H Amino acid Leucine Lysine Glutamic acid L-leucine L-lysine L-glutamic acid 2.36 2.18 2.19 pKa (α-NH3*) pKa (side chain) 9.60 8.95 9.67 10.79 4.25
4 An aqueous solution of an amino acid with a dissociable side chain is found to have the following side chain ratio at pH 4.0: K=[A- ]/[HA]=0.01. What is the identity of the amino acid?
Refer to the bar graph below, Explain why the n→π* interactions contributes more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though n→π* is the weaker interaction. Explain why that's the case for EACH of the bonds. I.e Why n→π* interactions contribute more to the overall stabilization of the protein than C-H-O hydrogen bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than π-π interactions even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than C5 Hydrogen Bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Cation-π interactions, even though…
Refer to the bar graph below, Explain why the n→π* interactions contributes more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though n→π* is the weaker interaction. Explain why that's the case for EACH of the bonds. I.e Why n→π* interactions contribute more to the overall stabilization of the protein than C-H-O hydrogen bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than π-π interactions even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than C5 Hydrogen Bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Cation-π interactions, even though…
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.
4. For the Amino Acid you have been assigned, at the pH values provided, draw the structure(s) at each of the specified pH values. serine and pH = 0, 7, and 9 5. What is the overall charge for each of the structures you drew?
Answered proteln structure 1 Which is an example of primary protein structure? Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer a. Multiple folded protein chains create an overall shape of a protein complex, b Amino acids form a particular sequence of residues A protein contains many alpha helices. A protein folds around itselrto exposehydrophilic groups on its surface
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.