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…

Chemistry & Chemical Reactivity

9th Edition

ISBN:9781133949640

Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Publisher:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Chapter24: Biochemistry

Section24.1: Proteins

Problem 3RC

See similar textbooks

Similar questions

The chemical structure of cysteine (C3H-NO₂S) is shown below. Highlight each atom that is in an amino group. :S H | HC-H H-C | H-N-H :0: || C. -0-H X 5 Save For Late
22-59 What is the effect of salt bridges on the tertiary structure of proteins?
Direction: Identify the type of IMFA on the following pairs of molecules Pairs of Molecules Type of IMFA 1) HF--HF Dipole-dipole, H-bonding 2) KCI----КСІ 3) СНЗОН-—-СНЗОН 4) CиО——Cи 5) SÜH3--SbH 6) Na2S--Na2S 7) NH3–-NH3 8) HBr and H2S 9) Cl2 and CBr4, 10) I2 and NO3- 11) NH3 and C6H6
The amino acid histidine has ionizable groups with pKa values of 1.8, 6.0, and 9.2, as shown. COOH H₂N-CH CH₂ H 2 -N H lonizable group 6.0 1.9 7.94 0.11 N H CH -COOH H₂N-CH | CH₂ H 2 N 1.8 COO- I pk₁ C H COO- CH -HisH+ H₂N-CH 6.0 COO- pk ₂. CH₂ H 2 H -His N CH COO™ H₂N-CH 9.2 pk 3 CH₂ H -N с H —NH — —NH, A biochemist makes up 95 mL of a 0.11 M solution of histidine at a pH of 5.1. She then adds 60 mL of 0.10 M HCI. What is the pH of the resulting solution? N CH
9. Which of the following non-covalent interactions could the sidechain of F266 participate in. Place an "X" next to all that apply. lonic (or salt bridge or charge-charge) Hydrogen bond Dipole-dipole Dipole-induced dipole Induced dipole-induced dipole Charge-dipole Charge-induced dipole П-stacking 10. The thermodynamic values for the folding of a protein are as follows: AG° = -38 kJ/mol = AH° = -164 kJ/mol AS -0.68 kJ/K.mol Which one of the following statements is most likely true? Circle your answer. A. Folding of this protein is primarily driven by the formation of favorable noncovalent interactions in the folded protein. B. Folding of this protein is primarily driven by the formation of hydrogen bonds between the protein and the bulk solvent (water). C. Folding of this protein is primarily driven by the loss of conformational entropy in the folded protein. D. Folding of this protein is primarily driven by the gain of conformational entropy in the folded protein. E. Folding of this…
Hello I just wanted to check my answers and get additional information. For 2B I have the same structure as the first but instead of OH I just have S
Which of the following are examples of isobars? S-40 & CI-40 S-32 & P-31 Na-37 & K-39 C-12 & C-14
Write down the Structure Activity Relationship(SAR) of Tricyclic Antidepressant(TCA)
provide brief explanation thnks
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…
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…
Match the following amino acids with their chemical properties H -N-CIC- A -A ✓ B но с D VE ✓ F ✓ G / CH3 CH3 CH B H но -N-C-C- feed C но -N-C-C- H CH₂ D HO -N-CIC- 1 H CH₂ OH E но ||| -N-C-C- II H CH₂ I CH₂ CH₂ CH₂ T NH3 I. Acidic II. Nonpolar III. Polar uncharged IV, Basic + F O HO -N-C-C- H CH₂ NH₂ G но | || -N-C-C- I H CH₂ 1

SEE MORE QUESTIONS

Recommended textbooks for you

Chemistry & Chemical Reactivity

Chemistry

ISBN:

9781133949640

Author:

John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Publisher:

Cengage Learning

Introduction to General, Organic and Biochemistry

Chemistry

ISBN:

9781285869759

Author:

Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:

Cengage Learning

Organic Chemistry: A Guided Inquiry

Chemistry

ISBN:

9780618974122

Author:

Andrei Straumanis

Publisher:

Cengage Learning

Chemistry & Chemical Reactivity

Chemistry

ISBN:

9781133949640

Author:

John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Publisher:

Cengage Learning

Introduction to General, Organic and Biochemistry

Chemistry

ISBN:

9781285869759

Author:

Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:

Cengage Learning

Organic Chemistry: A Guided Inquiry

Chemistry

ISBN:

9780618974122

Author:

Andrei Straumanis

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS