Forces involved in protein folding include:
1- hydrogen bonding, hydrophobic interactions and electrostatic interactions.
2-hydrophobic interactions
3- electrostatic interactions.
4-hydrogen bonding.
5- only hydrogen bonding and electrostatic interactions.
Forces involved in protein folding include: 1- hydrogen bonding, hydrophobic interactions and electrostatic interactions. 2-hydrophobic interactions...
Which of the following forces affect protein conformation: (May be more than one answer) a.)Hydrogen Bonds b.)Electrostatic attractions c.)Van der Waals interactions d.)Hydrophobic effect e.)Covalent Bonds
Which of the following is true of secondary structure in protein folding? Pick ALL that apply. A. It involves hydrogen bonding. B. It involves the side chains. C. It involves hydrophobic interactions. D. It results in alpha helicies with the side chains hidden inside the helix. E. It results in beta-pleated sheets with side chains sticking out of the plain of the sheet. F. It involves the peptide backbone.
How does the hydrophobic effect influence protein folding? In an aqueous environment, nonpolar portions of the molecule A) are generally exposed to solvent and interact effectively with water. B) interact with polar portions in the interior of the protein. C) can be placed on the surface of the molecule only if hydrogen bonded to water. D) are found in the interior of the protein, away from water, which preserves the entropy of water in solution.
25) What maintains the secondary structure of a protein? a) hydrophobic interactions b) hydrogen bonds between the R groups c) peptide bonds d) disulfide bonds e) hydrogen bonds between the amino group of one peptide bond and the carboxyl group of another peptide bond
CHEMWORK Considering only the compounds without hydrogen bonding interactions, which compounds have dipole-dipole intermolecular forces? (Select all that apply.) ON₂ О НЕ HO SF HBO SF Submit
Biochem- please answer all You need to denature a heterodimeric protein that uses both ionic interactions and hydrophobic forces to hold the dimers together. Each subunit has 2 disulfide bonds that hold their 3 structures together. One subunit is primarily composed of P-Sheets while the other has multiple helix-strand-helix motifs. The subunit with the helix-strand-helix also has a number of polar and charged residues on its surface. What would you do to denature this protein and which NCI would be...
identfiy the predominant intermolecular forces in each of the given substance Ionic interactions hydrogen bonding van der waals interactions Answer Bank KCI NH, CH П н, сн, Н,0 но СН3СНОН H. Urea is an organic compound widely used as a fertilizer. Its solubility in water allows it to be made into aqueous fertilizer solutions and applied to crops in a spray. What is the maximum theoretical number of water molecules that one urea molecule can hydrogen bond with? Ignore shape...
O points 1 attempts left Check my work What interactions are responsible for maintaining quaternary protein structure? Select all that apply O ionic bridges van der Waals forces hydrogen bonding O disulfide bonds peptide bonds
Question 3 (1 point) Hydrogen bonding is based on the electrostatic interaction. O True O False
2) At a pH greater than that of its isoelectric point, the structure of glycine is a) H-CH-COOH b) H-CH-C00- c) H-CH-CO e) H-CH-COO COOH b) H-CH-C00- c) H-CH-COOH d) H-CH-COO NH2 NH2 NH2 NH3 NH 3) Which of the following structures can be destroyed by the dena structures can be destroyed by the denaturation of a protein? a) Only primary and tertiary structures of a protein. b) Only secondary, tertiary y secondary, tertiary, and quaternary structures of a protein....