ionic bondhydrogen bondAnswer Bankhydrophobic interactiondisulfide bondIdentify the major force controlling tertiary protein structure.disulfide bondshydrogen bondinginorganic ionsion pairsOhydrophobic effect-CH-NHO-C-CH2-CH3HCHO-CH2CH3-CH2-S-S-CH₂-CH3 H3CCHCH-CH3 H3COH-CH2-C=OHO-CH₂-ΗΝ.OH-NR-CΝΗC=OC-R

The major force controlling the tertiary structure of proteins is the hydrophobic effect. This force…

Answered: ionic bond hydrogen bond Answer Bank…

Introductory Chemistry: An Active Learning Approach

6th Edition

ISBN:9781305079250

Author:Mark S. Cracolice, Ed Peters

Publisher:Mark S. Cracolice, Ed Peters

Chapter22: Biochemistry

Section: Chapter Questions

Problem 11E: Describe in words the hydrogen bonding that occurs in a protein having an -helix secondary...

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a 3d structure of protein with acces number of P02008 at uniprot database.
The denaturing of proteins occurs when the stabilizing forces are altered. Below is the set of processes in which proteins are denatured. Classify the following processes according to the denaturing agent involved. Please help me understand the diff and correct any mistakes.
A protein has a number of aspartyl and gluatmyl residues, what would be the expected pI for this protein? a. Basic pI b. Neutral pI c. Cannot be determined d. Acidic pI
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. Why n→π* interactions contribute more to the overall stabilization of the protein than Sulfur-arene interactions, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Anion-π interactions, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Chalcogen bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than X-H-π interactions, even…
Although the bond energy for the hydrogen bond in a vacuum is estimated to be about 20 kJ/mol, we find that each hydrogen bond in a folded protein contributes much less--probably less that 5 kJ/mol--to the enthalpy of protein stabilization. Suggest an explanation for this difference. Explain briefly.
A peptide has the sequence Glu–His–Trp–Ser–Gly–Leu–Arg–Pro–GlyGlu–His–Trp–Ser–Gly–Leu–Arg–Pro–Gly The p?a values for the peptide’s side chains, terminal amino groups, and carboxyl groups are provided in the table. Amino acid Amino pKa Carboxyl pKa Side‑chain pKa glutamate 9.609.60 2.342.34 4.254.25 histidine 9.179.17 1.821.82 6.006.00 tryptophan 9.399.39 2.382.38 serine 9.159.15 2.212.21 glycine 9.609.60 2.342.34 leucine 9.609.60 2.362.36 arginine 9.049.04 2.172.17 12.4812.48 proline 10.9610.96 1.991.99 Calculate the net charge of the molecule at pH 8
A peptide has the sequence Glu–His–Trp–Ser–Gly–Leu–Arg–Pro–Gly The p?a values for the peptide’s side chains, terminal amino groups, and carboxyl groups are provided in the table. Amino acid Amino pKa Carboxyl pKa Side‑chain pKa glutamate 9.609.60 2.342.34 4.254.25 histidine 9.179.17 1.821.82 6.006.00 tryptophan 9.399.39 2.382.38 serine 9.159.15 2.212.21 glycine 9.609.60 2.342.34 leucine 9.609.60 2.362.36 arginine 9.049.04 2.172.17 12.4812.48 proline 10.9610.96 1.991.99 Calculate the net charge of the molecule at pH 11 and estimate the isoelectric point (pI)(pI) for this peptide.
Identify the predominate attractive force responsible for the protein's tertiary structure at the location circled in red.
Identify the predominate attractive force responsible for the protein's tertiary structure at the location circled in red. Select one: H- bonding Covalent Dispersion Dipole-dipole Ionic
Which peptides is more likely to take up on alpha-helical structure? Explain. Top: Leu-Lys-Ala-Glu-Asn-Asp-Glu-Ala-Ala-Arg-Ala-Met-Ser-Glu-Ala Bottom: Cys-Arg-Ala-Gly-Gly-Phe-Pro-Trp-Asp-Gln-Pro-Gly-Tyr-Ser-Asn
Almost all proteins are composed from a set of about _____ amino acids.a. 4b. 10c. 20d. 50 ______ amino acids are considered essential.a. 5b. 10c. 15d. 20 An amino acid that has an indole group side chain.a. Trpb. Phec. Tyrd. ProWhich of the following is the simplest amino acid?a. Alab. Glyc. Vald. ProWhich of these will not give a blue solution with Ninhydrin testa. Prob. Phec. Alad. CysA neutral molecule with a positive and negative electrical charge.a. Isoelectric pointb. Zwitterionsc. Bufferd. Amphoteric3 amino acids joined together by two peptide bonds.a. Dipeptideb. Tripeptidec. Tetrapeptided. PolypeptideAn amino acid that can form disulfide bondsa. Cysteineb. Methioninec. Cystined. SerineWhich of the following is not a property of amino acidsa. Bufferb. Isoelectric pointc. Zwitterionsd. Insoluble in waterThe protein primary structure is held together bya. Hydrogen bondsb. Disulfide bondsc. Peptide bondsd. Protein bonds

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