Life: The Science of Biology
11th Edition
ISBN: 9781319010164
Author: David E. Sadava, David M. Hillis, H. Craig Heller, Sally D. Hacker
Publisher: W. H. Freeman
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Chapter 3.2, Problem 1R
Summary Introduction
To review:
The occurrence of change in the tertiary or the secondary structure of protein on replacement of one lysine residue by aspartic acid and the mechanism of this replacement.
Given:
One lysine residue is replaced by an aspartic acid residue in the protein.
Introduction:
The alteration in the primary structure takes place on replacement of one amino acid with another. The aspartic acid has negative change due to the presence of −COO− (carboxyl group) and the lysine has positive change due to presence of −NH3 (amino group). Amino acids that were initially bonded to aspartic acid get detached and new amino acids bind to the lysine residues on the replacement of aspartic acid with lysine.
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In regards to the protein structure, explain what is meant by “tertiary structure.” Whatare the main forces that stabilize tertiary structures in proteins? Provide examples.
Why is the ionic bond between, say, the side chain of lysine and the side chain of glutamic acid stronger in the hydrophobic interior of a protein than in aqueous solvent (water)?
At what level of protein structure (primary, secondary, tertiary or quarternary) does Hydrogen bonding is relevant ? Consider if there is no Hydrogen bonding that exists, and only van der Waals exists in this protein structure, what do you expect to happen in its property? Explain with examples.
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- Describe the two types of secondary structure apolypeptide can attain. Which proteins can achievequaternary structure? Which protein structure(s) are alteredby denaturation?arrow_forwardOccasionally, gaps are found in the crystal structure. How should one interpret the structure at these points, or proceed if these amino acids are missing?arrow_forwardResidues such as valine, leucine, isoleucine, methionine, andphenylalanine are often found in the interior of proteins,whereas arginine, lysine, aspartic acid, and glutamic acid areoften found on the surface of proteins. Suggest a reason forthis observation. Where would you expect to find glutamine,glycine, and alanine?arrow_forward
- Which kinds of interactions can be seen in the tertiary structure of proteins?arrow_forwardDiscuss and identify the four levels of protein structure (primary, secondary, tertiary,and quaternary). Explain how the structure of a protein affects its properties and howdenaturation changes the structure.arrow_forwardif glutamic acid were replaced by proline in a protein, how would the tertiary structure be affected?arrow_forward
- Each amino acid in a run of several amino acid residues of a polypeptide chain have phi values of approximately -140° and psi values of +147°. What kind of structure is this likely to be?arrow_forwardis Tertiary protein structure come from secondary structure？How are they related？（do we need to build up a secondary structure before make it become tertiary？）arrow_forwardGenerally speaking, what two considerations determine whether a specific dihedral angle will be permitted to exist in a protein?arrow_forward
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