Where would the leucine side chain most likely be found in a protein dissolved in water? In the interior of the protein in contact with polar side chains On the exterior of the protein On either the interior or the exterior of the protein In the interior of the protein in contact with nonpolar side chains In the interior of the protein in contact with water

Where would the leucine side chain most likely be found in a protein dissolved in water? In the interior of the protein in contact with polar side chains On the exterior of the protein On either the interior or the exterior of the protein In the interior of the protein in contact with nonpolar side chains In the interior of the protein in contact with water

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter3: The Chemistry Of Life: Organic Compounds

Section: Chapter Questions

Problem 9TYU: Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary...

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Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternary
Figure 3.23 Which categories of amino acid would you expect to find on the surface of a soluble protein, and which would you expect to find in the interior? What distribution of amino acids would you expect to find in a protein embedded in a lipid bilayer?
An N-linked glycoprotein contains a glycan covalently linked to which specific amino acid in a protein? Asparagine Glutamine Threonine Serine
A protein that is normally found in an aqueous solution has these amino acids in its primary structure: glutamic acid, lysine, leucine, arginine, and tryptophan. Predict the location of each amino acid: in the interior portion of the protein (away from water) or on the outside of the protein (facing water). glutamic acid _________________________ lysine _________________________ leucine _________________________ arginine ________________________ tryptophan _________________________
When a protein is folded in aqueous solution, some residues are driven inside to form a “hydrophobic core” which is far away from the water molecule. Which pair of the following residues are likely to be in the “hydrophobic core”? a. Gln and His b. Thr and Val c. Asp and Arg d. Ser and Tyr e. Ile and Leu
Which of the following statements concerning complete protein hydrolysis is incorrect? Primary structures are preserved Tertiary and secondary structures are disrupted All peptide bonds are broken Water is a reactant in the process
After denaturation of a tertiary protein like lysozyme (with one polypeptide chain), the only remaining bonds between its monomer subunits will be: the disulfide bonds the van der Waals forces the peptide bonds the hydrogen bonds the ionic bonds
Which of the following amino acids is most likely to be found on the outside of a soluble protein? Which is more likely to be found on the inside? Explain each answer. (Hint: Consider the effect of the amino acid side chain in each case and that the protein is folded up into its globularform.)(a) Leucine (b) Glutamate(c) Phenylalanine (d) Glutamine
Proper folding is essential for most proteins to function. Which of the following statement about protein folding are correct. There may be more than 1 right answer. a) changing the primary sequence will change the final conformation b) desaturation results in a protein that has a higher free energy than the native conformation c) protein spontaneously fold into their correct shape d) denatrutation will cause a protein to lose its tertiary structure
At what level of protein structure (primary, secondary, tertiary, or quaternary) will protein structure be initially altered? A mutation in the genetic sequence, which ultimately causes an amino acid to change(e.g. Trp – Asn – His turns into Trp – Arg – His) Dissolving a protein in a non-polar solvent (like oil) instead of water.
Which of the following is an example of protein denaturation? * A. Amino acids fold into repeating patterns due to hydrogen bonding of the peptide backbone. B. Several amino acids are joined together together via peptide bonds. C. A protein binds with with a substrate, lowering the activation energy of reaction. D. A protein is exposed to extremely high heat, causing it to lose its secondary structure and be left with only its primary structure. E. Results to unfolding, partial or incomplete disorganization of the protein's secondary and tertiary structure.
Which of the following statements are correct about the native state of a protein (select all that apply)? A. Polar sidechains commonly interact with water B. Hydrophobic amino acids tend to be on surface of protein C. The sidechains of polar amino acids are most commonly found in the central core of a protein D. Formation of an alpha-helix is primarily driven by hydrogen bonds between the protein main chain, not sidechains. E. Secondary structure is largely driven by hydrophobic interactions