Describe in no more than 10 sentences the four levels of protein in structure and cite the noncovalent forces in each level
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- Describe in no more than ten sentences the four levels of protein structure, and cite the non-covalent force(s) in each level.Describe in no more than ten sentences the four levels of protein structure, and cite the noncovalent force(s) in each.Give at least 10 functions of protein and describe each function. Cite an example for each function if there are any.
- Please describe the non-covalent interactions that exist in protein solution (proteins were dissolved in water) and describe their characteristics.Name and discuss the non-covalent interactions that maintain protein structure. Explain the chirality of amino acid molecules.Protein structure: a). Name the four levels of protein structure, b). Describe the structural characteristics at each level, C. For one protein describe how "A" and "B produce the effects that the protein produces
- Label: 1) the type of chemical bonds between the amino acids (e.g. covalent bond, ionic bond, metallic bond) 2) the type of interparticle forces of attraction occurring within the protein and with its environment *Indicate at least four observed interparticle forces of attraction *pink - negatively charged, blue - positively charged, yellow - nonpolar and uncharged, green - polar and uncharged *[See example picture] The chemical bond (shown by the arrow) is depicted as a line between the amino acids. Interparticle forces of attraction, such as the one between Phe and Glu (boxed), are not represented by lines but rather by the proximity of amino acids.In the following diagram of a portion of a protein, label the types of interactions that are shown. What level of protein structure are these interactions producing? ____________________Explain the concept of protein folding and its importance in determining protein structure and function.
- Discuss the different structures (primary, secondary, tertiary, and Quaternary structures) of protein. What are the five factors that promote protein folding and stability. (Hint: One factor is the Hydrogen bond). Extra Hint: Another factor is the Hydrophobic effect.In general, proteins can be classified into 3 different groups. Name and give a short description of each type and how they are distinct from one another. Provide an example of macromolecule or other complex structure representing each of the three types.The addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.