Chemistry 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. Here's what R₁ looks like:-CH-ICH3CHCH3Could R₁ form a salt bridge with R, at physiological pH, if R2 were the right kind of residue?If you said R₁ could form a salt bridge 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 the3-letter code of any of them.yesno

An α-helix is a protein structure where the primary chain of the protein forms a spiral staircase…

Answered: Imagine the main chain of a protein…

Organic And Biological Chemistry

7th Edition

ISBN:9781305081079

Author:STOKER, H. Stephen (howard Stephen)

Publisher:STOKER, H. Stephen (howard Stephen)

Chapter9: Proteins

Section: Chapter Questions

Problem 9.58EP

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Using both three- and one-letter codes for amino acids, write the structures of all possible peptides containing the following amino acids: (a) Val, Ser, Leu (b) Ser, Leu2, Pro
How many of the -amino acids shown in Table 26-1 contain aromatic rings? How many contain sulfur? How many contain alcohols? How many contain hydrocarbon side chains?
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. Here's what R₁ looks like: HO -CH- | CH CH3 Could R₁ form a hydrogen bond with R, at physiological pH, if R₂ were the right kind of residue? If you said R₁ could form a hydrogen bond with R₂, what would R, 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. ☐ yes no
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. Here's what R₁ loo -CH- CH₂ CH₂ CH₂ NH H₂N NH₂ Could R₁ form a salt bridge with R, at physiological pH, if R₂ were the right kind of residue? O yes O no If you said R₁ could form a salt bridge with R₂, what would R₂ have to be? 0 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. X
H. H. H. CH2 (CH2)4 NH3* CH2 но CH CH, CH CH2 CH2 H. (a) (b) (e) Which of the interactions stabilizing protein tertiary structure is (a)? O hydrophobic interaction O disulphide bridge bonding O hydrogen bonding O salt bridge bonding
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. Here's what R₁ looks like: -CH- HO CH CH3 Could R₁ form a hydrogen bond with R₂ at physiological pH, if R₂ were the right kind of residue? If you said R₁ 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. yes X © no G
What type of chemical bond stabilizes the protein secondary structure, such as the alpha helix shown below. O Hydrogen bond O Salt bridge O Hydrophobic interaction O Disulfide bridge U=O....H -Z U=O... HIZ 010 HIN ····HINI CIO....H C=O... H
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.
8. The following proteins represent a wide range of molecular weights and isoelectric points. Mr is the molecular weight of a single protein chain. • Protein 1: Mr 68,544; pl 6.11 (monomer) • Protein 2: Mr 29,041; pl 5.32 (dimer) • Protein 3: Mr 15,805; pl 5.7 (dimer) • Protein 4: Mr 12,165; pl 4.74 a. Which protein is the most acidic? Explain your answer. b. Which protein will migrate the slowest in an SDS-PAGE? Explain your answer. c. In what order will these proteins elute from a cation exchanger at pH 8? Explain your answer. d. In what order will these proteins salt out from a pH 7 solution by the dropwise addition of saturated ammonium sulfate? Explain your answer. 5 83°F Cloudy
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…
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 residues. If a specific interaction could form, give the name of the interaction. R₁ R₁₂ specific interaction? name of specific interaction X 5 O yes O valine phenylalanine 0 О по O yes threonine tyrosine 0 O no O yes lysine glutamate 0 O no O yes phenylalanine serine Π O no Explanation Check Vicoran Hill LLC. All Rights Reserved. Terms of Use Privacy Center
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.

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