'negatively-charged aspartic acid side chain and a positively charged lysine side chain on the surface of a protein structure are separated by a center-center distance of 5 A in aqueous buffer.'
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What is aspartic acid and lysine? Aspartic acid and lysine are amino acids, which are the building blocks of proteins. They have different chemical properties and can interact with each other in various ways. Show more…
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Consider a side chain attraction between aspartic acid and lysine that holds a protein's tertiary structure together. If the pH near this attraction is greatly increased, some denaturation may occur because: The NH3+ group on lysine's side chain will be deprotonated. The COO- group on aspartic acid's side chain will be protonated. The COO- group on aspartic acid's side chain will be deprotonated. The NH3+ group on lysine's side chain will be protonated.
Madhur L.
4. The pKa of an amino acid's side chain is influenced by its local environment. Predict the effect of each of the following local environments on the pKa of a glutamic acid side chain: (2 points) A. A lysine side chain is brought into close proximity. B. The carboxyl terminus of the protein is brought into close proximity. C. The glutamic acid side chain is moved from the surface of the protein to the nonpolar interior of the protein.
Sri K.
Draw a diagram of the lysine side chain in the protonated and unprotonated state. Calculate the ratio of the protonated and unprotonated forms of this side chain that would exist at pH 7 (assume pKa = 10).
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