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.1In the table below are four possibilities for what R₁ and R₂ might be. In each case, decide whether a specific interaction could form between the residues. If aspecific interaction could form, give the name of the interaction.R₁specificinteraction?R₂○ yeslysineglutamatenoname of specificinteraction☐threoninethreonine○ yes○ noleucineglutamine○ yesO no○ yescysteinecysteineO no

Lysine (R) and Glutamate (R):Interaction: Hydrogen bond can form.Reason: The side chain of lysine…

Answered: Imagine the main chain of a protein…

Introduction to General, Organic and Biochemistry

11th Edition

ISBN:9781285869759

Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Chapter22: Proteins

Section: Chapter Questions

Problem 22.68P

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Imagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R₂ come close to each other. In the table below are four possibilities for what R, and R₂ might be. In each case, decide whether a specific interaction could form between th residues. If a specific interaction could form, give the name of the interaction. R₁ R₂ specific interaction? name of specific interaction X 5 O yes valine phenylalanine hydrogen bonding O no O yes threonine tyrosine hydrogen bonding O no O yes lysine glutamate O no phenylalanine serine O yes О по O Explanation Check 3 W E R % 5 7 8 LLC. All Rights Reserved Terms of Use Privacy Comer G H K Z X V B N M alt H option cmd P H alt cmd op
Identifying specific interactions between residues in a protein 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 R, and R₂ might be. In each case, decide whether a specific interaction could form between the residues. If a specific interaction could form, give the name of the interaction. A Z R₁ R₂ specific interaction? name of specific interaction O yes cysteine cysteine 0 О по O yes Isoleucine O asparagine O no O yes lysine glutamate 0 O no O yes alanine isoleucine O O no Explanation Check 3 W E R alt option cmd H 5 6 8 H 5 ILLC. All Rights Reserved. Terms of Use Privacy Center Accessib V B N M дв cmd P alt option
Complete the table for the ionizable groups of the fictitious amino acid hypothetinine. Group alpha-amino alpha-carboxyl Ka 5.24 x 10-⁹ 2.13 x 10-3 pKa (to TWO decimals) 8.9 2.7 Average charge of group when pH=pK (to ONE decimal) -0.5 +0.5
H₂N Combination of two or more protein units 7. Which type of cross-link involves interactions between two cysteine amino acids? 8. Which type of cross-link would form between the following amino acids? Η Ο || H₂N-C-C-OH T CH₂ C=O NH₂ Η Ο LL H₂N-C-C-OH T CH₂ OH 9. To what main enzyme class do the nzym that catalyze the following reaction belong? (oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases) HO | || I c-c-N-C-COO + H₂O IT HR₂ R₁ H 1 This bond is cleaved H H₂N-C-COOⓇ I R₂ Wilter navy q H I H₂N-C-C00 1 R₁ •Qisulfide 10. Briefly explain the Lock and Key enzyme model.
The image below is a positive ionization mode Electrospray ionization-mass spectrum (ESI-MS) spectrum for a peptide, obtained using high resolution mass spectrometry. If ionization occurs through de-protonation (assuming that the mass of a proton is 1.0 Da), what is the neutral mass of the peptide, in Da? 627.271 627.604 100 - 627.938 628.271 628.604 628.938 627.0 628.0 629.0 mass/charge (m/z) 628.271 626.271 1878.813 O 1884.813 % Abundance
Question 2. While internal cysteine amino acid sidechains in proteins undergo oxidation to produce disulfide crosslinks that stabilize the protein structure after folding, solvent-exposed cysteine sidechains can remain in their reduced thiol form and serve as reactive nucleophiles (recall for instance Acyl Carrier Proteins involved in fatty acid biosynthesis or various oxidoreductase enzymes). The reactive thiol groups in proteins can be detected using Ellman's test, wherein the protein is reacted with a disulfide Ellman's reagent to form a new mixed disulfide and a 2-nitro-5-thiobenzoate (TNB) byproduct. Upon addition of base, TNB is deprotonated to form a dianion, which absorbs light in the visible region and can be detected using UV-Vis spectroscopy. Ellman's Reagent CO₂H -NO₂ internal disulfide crosslink O₂N- HO₂C SH solvent- exposed thiol UV Absorbance at 412 nm O₂N- -S TNB²- alkaline pH O₂N- SH HO₂C 2-nitro-5-thiobenzoate (TNB) -NO2 mixed disulfide CO₂H a) Provide a detailed…
Refer to the bar graph below, Explain why e.g. the n→π* interactions contribute 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 they contribute more than EACH bond.
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…
Which of the following statements describes the amino acid presented below? ОН CH2 O HN — CH—С-о This amino acid contains a polar "R" group and and it is hydrophilic. This amino acid contains a nonpolar "R" group and and it is hydrophobic. This amino acid contains a nonpolar "R" group and and it is hydrophilic. O This amino acid contains a polar "R" group and and it is hydrophobic.
ogical Marcomalee Identifying specific interactions between residues in a protein 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 OH O yes Could R, form a hydrogen bond with R₂ at physiological pH, if R₂ were the right kind of residue? O no If you said R, could form a hydrogen 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. 0 Explanation Check ㅎ C S A * 2 # 3 $ 4 Z W M S X Ő % Λ 25 & 6 7 E R T Y U D C dill LLC. All Rights Reserved. Terms of Use Privacy Center NP 8 A 9 O 0 LL F G H J K L V B N M P alt
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.

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