Disulfide bonds between cysteine amino acids in a peptide chain are critically in stabilizing preferred secondary and tertiary structures. Many enzyme activities rely on specific shapes that are stabilized by these disulfide bonds.
Could depend on what your options are but out of my multiple choice answers this was the best:two cysteine residues.
The change in a proteins' three dimensional shape or conformation is called denaturation.
"b -mercaptoethanol is used to help to destroy RNases that may be present and will degrade the RNA. b -mercaptoethanol is a reducing agent that will reduce the disulfide bonds of the RNases, thereby destroying the conformation and the functionality of the enzyme". It comes from http://www.norgenbiotek.com/index.php?id=faqs_rnakits
SH-SH
Tertiary
The functional groups involved in forming disulfide bonds are sulfhydral (-SH) groups.
The functional groups involved in forming disulfide bonds are sulfhydral (-SH) groups.
Disulfide bonds
A disulfide bridge involves covalent bonds
Side bonds link two adjacent chains of atoms in a molecule. The three types of side bonds are hydrogen bonds, salt bonds and disulfide bonds.
Cysteine forms disulfide bonds
3
salt , hydrogen , and disulfide bonds
Yes, heavy metals insert themselves between disulfide bonds and this can cause denaturation of quaternary and tertiary protein structures.
Lanthionization is the process by which hydroxide relaxers permanently straighten hair. It breaks the hair's disulfide bonds during processing and converts them to lanthionine bonds when the relaxer is rinsed from the hair. Disulfide bonds contain two sulfur atoms. Lanthionine bonds contain only sulfur atom. The disulfide bonds that are broken by hydroxide relaxers are broken permanently and can never be re-formed.
Salt bonds, hydrogen bonds, disulfide bonds
Disulfide bonds