Explain protein-protein interactions too weak to assemble proteins in solution can allow the same proteins to assemble into complexes on DNA.

Mass spectrometry and X‑ray diffraction are common biochemical techniques for characterizing proteins. Classify each statement based on whether it applies to mass spectrometry, X‑ray diffraction, or both techniques.

Rank these molecules in order of increasing energy state (1 = lowest energy; 4 = highest energy) Partially folded protein Completely denatured protein Native conformation protein Aggregated amyloid proteins [Choose ] [Choose ] [Choose] [Choose ]

A. What change should disrupt the interaction between proteins 1 and 2 the most? Why? B. What change would disrupt the interaction between proteins 1 and 2 the least? Why?

Explain how the lipid bilayer modulate the activity of proteins. Give 2 examples.

D. Draw the structure of Histidine and Imidazole. Why do you think we use Imidazole to elute the protein? Why do we use a 6X His tag?

Protein Structure and Folding:a. Explain how changes in a protein’s amino acid sequence can change the way it behaves in water.b. Explain how changes in a protein’s amino acid sequence can change the way it interacts with othermolecules.c. Explain how changes in a protein’s amino acid sequence can change the way it forms secondary andtertiary structures when placed in water.

Describe how a carrier protein functions. What role do carrier proteins serve in the cell? Why are they necessary? Where might you find a carrier protein?

Briefly explain how an epitope can be used to study how many subunits are in a protein complex.

Affinity and specificity of protein-protein interactions are mainly mediated by many weak chemical bonds such as: Group of answer choices   van der Waals forces   hydrogen bonds   hydrophobic interactions   all of the above