Which amino acids interact with DNA backbone?
One part of the domain contains a region that mediates sequence specific DNA binding properties via basic amino acids such as arginine and lysine. These basic residues can either interact ionically with the negatively charged backbone phosphate groups or via hydrogen bonds with the bases.
What four types of interactions maintain the tertiary structure of a protein?
There are four types of tertiary interactions: hydrophobic interactions, hydrogen bonds, salt bridges, and sulfur-sulfur covalent bonds.
Which interaction occurs between the side chains of arginine and glutamic acid?
ionic bond
The arginine amino acid side chain of protein 1 has a positive charge. The glutamic acid amino acid side chain of protein 2 has a negative charge. The most likely interaction between these two amino acids is an ionic bond, i.e. an attractive force between the positive and negative charge.
What is special about cysteine?
Cysteine is unique among coded amino acids because it contains a reactive sulph-hydryl group. Therefore, two cysteine residues may form a cystine (disulfide link) between various parts of the same protein or between two separate polypeptide chains.
How does DNA interact with amino acids?
Peptides and proteins may presumably interact with DNA in a similar manner whereby their amino acid composition will determine the stability of the double helix. When the peptide contains mainly negatively charged amino acid residues (Asp, Glu), DNA binds acidic peptides in major groove of double helix.
How do amino acids in DNA-binding proteins interact with DNA?
Direct recognition occurs when the amino acid side chains of a protein interact with specific DNA bases [6]. Most protein-DNA interactions are mediated by direct physical interaction (hydrogen bonding or hydrophobic interactions) between the protein and the DNA base pairs.
Does lysine and glutamic acid form hydrophobic interactions?
Lysine and glutamic acid form hydrophobic interactions . Upon hydrolysis the dipeptide abbreviated as Gly-Lys will yield the same products as the dipeptide abbreviated as Lys-Gly.
What are the main interactions that stabilize each level of protein structure?
Four interactions stabilize the tertiary structure of a protein: (a) ionic bonding, (b) hydrogen bonding, (c) disulfide linkages, and (d) dispersion forces.
Which amino acids can form hydrophobic interactions?
Hydrophobic Amino Acids The nine amino acids that have hydrophobic side chains are glycine (Gly), alanine (Ala), valine (Val), leucine (Leu), isoleucine (Ile), proline (Pro), phenylalanine (Phe), methionine (Met), and tryptophan (Trp). Shown at the right is the structure of valine.
Can serine and asparagine bond?
Serine, threonine, and asparagine are also the binding sites of carbohydrates that are attached to the surface of many proteins. Carbohydrates bound to serine and threonine form O-glycosidic bonds and those linked to asparagine form N-glycosidic bonds. Cysteine (Cys) carries the highly reactive sulphydryl group.
What are the side effects of cysteine?
Very high doses (more than 7 grams) of cysteine may be toxic to human cells and may even lead to death. Taking NAC by mouth may cause nausea, vomiting, and diarrhea. Intravenous administration of NAC to treat acetaminophen poisoning may cause severe allergic reactions, including: Angioedema.