In regards to the protein structure, explain what is meant by “tertiary structure.” What are the main forces that stabilize tertiary structures in proteins? Provide examples.
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In regards to the protein structure, explain what is meant by “tertiary structure.” What
are the main forces that stabilize tertiary structures in proteins? Provide examples.
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Solved in 2 steps
- Define the term isomer and distinguish among the three principal isomer types.What are some of the ways that the features of carbon-to-carbon bonds influence the stability and 3-D structure of organic molecules?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
- While abnormal physiological conditions such as high urea concentration and very high/low pH can affect proteins, can they affect the primary structure (peptide bonds and such)?Generally speaking, what two considerations determine whether a specific dihedral angle will be permitted to exist in a protein?What structural and functional advantages do proteins gain by associating to form quaternary structures?
- Because of their tendency to avoid water, nonpolar aminoacids play an important role in forming and maintaining thethree-dimensional structure of proteins. Can you suggesthow these molecules accomplish this feat?Why is cysteine such an important amino acid for defining the tertiary structure of some proteins?What Noncovalent Interactions Stabilize the HigherLevels of Protein Structure?
- Why is the 3-Dimensional structure important for protein function? What factors or agents can denature protein structure? Give examples (more than one factor) Why denaturation affect the function of proteins? Explain the structure - function relationship.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.Based on molecular weights of purified (no beta-Me) and (beta-Me) sample, which are 140 kDa and 72 kDa, what can be said about the number and size of the protein monomers, as well as the nature of the bonds holding together the complete quaternary structure of the proteins?
