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 following graph shows the activity versus pH curve for pepsin, an enzyme that breaks down proteins into smaller peptides. Estimate its optimum pH. Maximum activity No activity pH 0 pH 3.8 pH 2 O pH4 Pepsin 01 2 3 pH 4 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.
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…
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
Use the online JPRED 4 secondary structure prediction tool (Pred: A Protein Secondary Structure Prediction Server (dundee.ac.uk) to predict the secondary structure for the following input sequence: MNLVLMGLPGAGKGTQAEKIVAAYGIPHISTGDMFRAAMKEGTPL GLQAKQYMDRGDLVPDEVTIGIVRERLSKDDCQNGFLLDGFPRTV AQAEALETMLADIGRKLDYVIHIDVRQDVLMERLTGRRICRNCGAT YHLIFHPPAKPGVCDKCG GELYQRADDNEATVANRLEVNMKQMK PLVDFYEQKGYLRNINGEQDMEKVFADIRELLGGLAR How many helical regions are predicted? (Hint: see the View Simple Results in HTML). A 4 B 6 C O D 8 E 1
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…
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.
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
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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.

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