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-HOCHCH3Could 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 the3-letter code of any of them.yesX© noG

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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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 the residues. If a specific interaction could form, give the name of the interaction. R₁ R₂ specific interaction? name of specific interaction x yes alanine valine O no isoleucine asparagine ○ yes O no yes lysine glutamate ☐ O no yes threonine asparagine O no
Protein denaturation can alter the 3 dimensional shape of a protein alter the sequence of amino acids in protein Obreak the peptide bonds holding the protein together Other: What is the purpose of using enzyme in detergent industry? all of the statements are true Enzymes are used to remove protein stains O Enzymes are used to remove human sweat which have a tendency to adhere strongly on textile fibers O Enzymes are used to improve texture of cloth or fiber Other: When an enzyme becomes saturated with its substrate, the rate of reaction vs concentration of enzyme graph line becomes a plateau. To produce a significant change in the reaction rate O the pH must be decreased O the temperature must be increased O the concentration of the enzyme must be increased O the pH must be increased
Predict the most likely product of this biochemical reaction: CH₂= OH O + Pi X + H₂O That is, in the drawing area below, draw the chemical structure of the product molecule X. Note for advanced students: you can assume any necessary small-molecule reactants, like water, are available. Predicting reactants or products of phosphorylation Click and drag to start drawing a structure. X Ś (
For each of the following representations (from OpenStax Biology) indicate whether it is describing primary, secondary, or tertiary protein structure
H₂N CH3 ZI O OH Which of the following statements is True? SH ZI O OH NH₂ All amino acid residues are chiral. The C-terminus contains a basic residue. It cannot form disulfide linkage. The N-terminus is Ser. Assuming this is a DNA-encoded polypeptide, then all chiral centres are S.
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.
For the amino acid alanine, the major species in solution at pH 7 is the zwitterionic form, which has a negatively charged carboxylic acid group and a positively charged amino group. There is a less common neutral form in which neither group is charged. The carboxylic acid group of alanine has a p?a of 3 The amino group of alanine has a p?a of 8 Estimate the ratio of the concentration of the neutral amino acid species to the zwitterionic species at pH 7. __?__x10^?
All amino acids have two ionizable functional groups: an a-amino group (average pK, of 9.4) and an a-carboxylic acid group (average pK, of 2.2). Tyrosine also has an ionizable side chain (R group) with a pK, of about 10.1. One of the possible ionization states of tyrosine is shown. H3N-CH -C-OH CH2 ÓH At what pH would the structure be the predominant ionization state? Consider the ionization state of all three of the functional groups. The protonated form of the R group of tyrosine is shown in the structure. The ratio of the protonated form to the charged (deprotonated) form depends on the pK, of the R group and the pH of the solution. Select the pH value at which the charged form of the R group would predominate.
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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.
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
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