The tertiary structure of a protein is the 3-dimensional folding of the polypeptide chain. What types of bonds support the folding of proteins into this level of protein structure? Also, how do these bonds/interactions impact how a protein folds and its surface properties? Can the tertiary structure of a protein depend on the type of cell system used for synthesis? Explain

The tertiary structure of a protein is the 3-dimensional folding of the polypeptide chain. What types of bonds support the folding of proteins into this level of protein structure? Also, how do these bonds/interactions impact how a protein folds and its surface properties? Can the tertiary structure of a protein depend on the type of cell system used for synthesis? Explain

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter3: Biological Macromolecules

Section: Chapter Questions

Problem 2VCQ: Figure 3.23 Which categories of amino acid would you expect to find on the surface of a soluble...

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Many transmembrane proteins have a large series of hydrophobic amino acids such as those in the middle of the protein (around b). Why would this make sense, and where would you expect these to be located in the final protein structure?
Protein folding is critical for function because the properties of a protein arise from its overall shape and the distribution within that shape of the various amino acid side-chains. Which of the following statements about protein three-dimensional structure are correct? 1) the folding pattern of a protein is ultimately determined by its amino acid sequence. 2) proteins tend to fold in such a way that the hydrophobic amino acids are buried in the interior, while hydrophilic amino acids are exposed at the surface. 3) the chemical interactions within a protein molecule that support its overall folded structure are mostly covalent C-C (carbon to carbon) bonds between amino acid side-chains. 4) the overall folding pattern/shape of a protein molecule is termed its primary structure. 5) during evolution, the three-dimensional structure of a protein is often more strongly conserved than its amino acid sequence. More than one answer might be right
Non covalent bonds are very important in cell biology, could you explain why and provide an example that illustrates their importance ( do not chose protein folding as an example) What are the different levels of protein structure and what are the different parameters (sequence, type of bonds, etc...) that influence protein folding at these different levels?
Proper folding of proteins is essential for their biological activity. In general, the functional conformation of a protein is the conformation with lowest energy. This means that if an unfolded protein is allowed to reach equilibrium, it should assemble automatically into its native, functioning folded state. Why then is there a need for molecular chap- erones and chaperonins in cells? What different roles do molecular chaperones and chaperonins play in the folding of proteins?
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.
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? What does “polar” mean, in the case of an ionized molecule and how is this related to “charged” of a molecule? Explain the significance φ, ψ contour diagram in proteins and explore how is it interpreted?
Proper folding of proteins is essential for their biological activity. In general, the functional conformation of a protein is the conformation with lowest energy. This means that if an unfolded protein is allowed to reach equilibrium, it should assemble automatically into its native, functioningfolded state. Why then is there a need for molecular chaperones and chaperonins in cells? What different roles do molecular chaperones and chaperonins play in the folding of proteins?
it is widely accepted that proteins can organize themselves according to a range of stable structural motifs. How is this knowledge exploited in the organization of the protein data blank?
At what level of protein structure (primary, secondary, tertiary, or quaternary) will protein structure be initially altered? Heating a protein (due to fever), causing hydrogen bonds to break. Drastic changes in pH (like the above patients), causing some polar amino acids to turn into non-polar amino acids
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
a) Canonical forces in protein folding. Describe how these forces come into play when a protein folds. Why do are other intermolecular interactions important to fully understand folding processes?
Amino acids are ionic compounds, very soluble in water. Proteins, however, which are made up of amino acids are much less soluble, and must be folded up very precisely to maximize their solubility. Why are proteins so much less soluble than the amino acids of which they are made?