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Chapter 6: Problem 11

Which amino acids would be capable of forming H bonds with a lysine residue in a protein?

Short Answer

Expert verified
Amino acids capable of forming H bonds with a lysine residue in a protein include serine, threonine, cysteine, tyrosine, asparagine, glutamine, aspartate, and glutamate.

Step by step solution

01

Understanding Amino Acid Interactions

Amino acids interact with each other to form complex proteins. They do this through various types of bonds, one of which is a hydrogen bond. Hydrogen bonds form between a partially positive Hydrogen and a partially negative atom, typically Nitrogen or Oxygen.
02

Identifying Lysine Properties

Lysine is a basic amino acid with an –NH3+ group at its side chain’s end, which can act as a hydrogen donor. This means that it can form a hydrogen bond with any atom that can act as a hydrogen acceptor, i.e., an atom that carries a partial or full negative charge such as Oxygen or Nitrogen. Thus, looking for amino acids that have polar side chains involving Oxygen or Nitrogen will give us the answer.
03

Listing Amino Acids Capable of Forming H bonds

Amino acids with polar, uncharged side chains such as serine, threonine, cysteine, tyrosine, asparagine, glutamine will form H bonds with lysine. In addition, amino acids with negatively charged side chains like aspartate and glutamate are also likely to form H bonds with lysine.

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Most popular questions from this chapter

Imagine that the dimensions of the alpha helix were such that there were exactly 3.5 amino acids per turn, instead of \(3.6 .\) What would be the consequences for coiled-coil structures?

Discuss the potential contributions to hydrophobic and van der Waals interactions and ionic and hydrogen bonds for the side chains of Asp, Leu, Tyr, and His in a protein.

Poly-L-glutamate adopts an a-helical structure at low pH but becomes a random coil above pH \(5 .\) Explain this behavior.

Choose any three regions in the Ramachandran plot and discuss the likelihood of observing that combination of \(\phi\) and \(\psi\) in a peptide or protein. Defend your answer using suitable molecular models of a peptide.

Two polypeptides, \(A\) and \(B\), have similar tertiary structures, but \(A\) normally exists as a monomer, whereas \(\mathrm{B}\) exists as a tetramer, \(\mathrm{B}_{4}\) What differences might be expected in the amino acid composition of A versus B?
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