Intrinsically disordered proteins may:
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Question 39 options:
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lack a hydrophobic core.
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All of the answers are correct.
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wrap around their targets.
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have multiple interaction partners.
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- 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. Mass spectrometry protein must be conformationally stable X-ray diffraction small amounts of protein are sufficient analysis requires information about the protein-coding gene or genes Answer Bank protein may be denatured requires a large amount of protein protein sample must be pure can detect a covalent modification to a protein Both techniquesThe process of creating a polysaccharide can be referred to as: Question 18 options: polymerization polysaccharation glucosification macrolinkidationWhich statement is true regarding denaturation process? Question 21 options: Protein experiences hydrolysis as it denatures and alters its structure. Denaturation is the process of altering the shape of a protein that involves breaking the amide bonds. Denaturation is the process of altering the shape of a protein without breaking the amide bonds. As protein denatures, new peptide bonds form with the added amino acids.
- A protein that is normally found in an aqueous solution has these amino acids in its primary structure: glutamic acid, lysine, leucine, arginine, and tryptophan. Predict the location of each amino acid: in the interior portion of the protein (away from water) or on the outside of the protein (facing water). glutamic acid _________________________ lysine _________________________ leucine _________________________ arginine ________________________ tryptophan _________________________ Indicate whether each of the following statements describes a reversible competitive inhibitor, reversible noncompetitive inhibition, or an irreversible inhibitor. ________ a. It bonds covalently to the active site ________ b. The inhibitor effect can be reversed by the addition of more substrate ________ c. Inhibitor structure resembles that of the substrate ________ d. The inhibitor and substrate cannot bind to the enzyme simultaneously.A protein that is normally found in an aqueous solution has these amino acids in its primary structure: glutamic acid, lysine, leucine, arginine, and tryptophan. Predict the location of each amino acid: in the interior portion of the protein (away from water) or on the outside of the protein (facing water). glutamic acid _________________________ lysine _________________________ leucine _________________________ arginine ________________________ tryptophan _________________________Discuss the different structures of protein. What are the five factors that promote protein folding and stability. Explain your answers in depth and detail.
- true/ false: When proteins are denatured 1°, 2°, 3°, and 4° structure is lost.How can IDPs can gain a stable conformation? Question 45 options: By interacting with other proteins. They already exist in their final structure due to protein folding. By interacting with partially folded intermediates. By testing multiple partially stable intermediate structures to find the most energetically favourable structureDiscuss 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.
- The disulfide bonds that make up the tertiary structure of proteins are stabilized by hydrogen bonds. Select one: True FalseMass 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.Hydrogen bonds and hydrophobic interactions play important roles in stabilizing and organizing biological macromolecules. Describe how hydrogen bonds and hydrophobic interactions affect the form and function of proteins.