You are studying a peptide in the sky bison that has the sequence below. Ala-Met-Cys-Lys-Trp-Glu-Lys-Gln-Pro-Asp-Gly-Met-Glu-Cys-Ala-Phe Suppose this is a portion of the sequence of a large folded protein. Where in the protein would you expect to find the highlighted AAs? On the interior of the protein because these AA are nonpolar On the exterior of the protein because these AA are hydrophilic On the interior of the protein because disulfide bonds are nonpolar Not enough information to tell

You are studying a peptide in the sky bison that has the sequence below. Ala-Met-Cys-Lys-Trp-Glu-Lys-Gln-Pro-Asp-Gly-Met-Glu-Cys-Ala-Phe Suppose this is a portion of the sequence of a large folded protein. Where in the protein would you expect to find the highlighted AAs? On the interior of the protein because these AA are nonpolar On the exterior of the protein because these AA are hydrophilic On the interior of the protein because disulfide bonds are nonpolar Not enough information to tell

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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Proteins - Question Set I H2N- CH-C-NH- CH2-C-NH- CH2-C- NH-CH- C-NH-CH-C- OH CH2 CH2 CH2 CH Compound A (Leu-enkephalin) H3C CH3 OH 1. Name the individual amino acid residues which are present in Leu-enkephalin. 2. How many asymmetric centers are present in Leu-enkephalin and point out their location(s)? 3. Predict, with structures, the metabolic products produced from Leu-enkephalin.
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How many peptide bonds are in the below peptide O + HN-CH-CNH-CHC-NH-CH-c-o + CH₂ CH₂OH CH2(CH2)3NH3 2 1 3 4 OH
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…
1. Determine whether each of the following statements describes the primary, secondary, tertiary, or quaternary stucture of a protein. а. Peptide bonds join amino acids in a polypeptide chain. b. Two polypeptide chains are held together by hydrogen bonds. С. Hydrogen bonds form between adjacent segments of the backbone of the same protein to form a "folded fan" structure. 2. List the type of denaturing agent described by the following treatments: a. disrupting the disulfide bonds in hair to straighten it b. baking the proteins in dough to make bread
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
The tertiary structure of a protein is stabilized by several types of interactions between side chains. Classify the highlighted interaction (or bond) in each example. Answer Bank Hydrogen bond OH -CH,-C=O…HO-CH, Electrostatic interaction (ionic bond) 요 -CH,-NH, O-C-CH, OC-CH Hydrophobic interaction CH3 H3C -CH CH- CH, HẠC Disulfide bond -CH₂-S-S-CH₂-