Amino Acids 9. The tertiary structure of a Protein.

Sdílet
Vložit
  • čas přidán 10. 07. 2016
  • This video provides a quick overview of the 4 types of bond that hold a polypeptide molecule in its folded tertiary structure. It uses animation to show van der Waals forces form between adjacent valine molecules; electrostatic attractions form between lysine and aspartic acid; hydrogen bonds forming between the O-H of aspartic acid and O-H of serine; and a disulphide bond form between cysteine molecules. These bonds explain why the polypeptide should take on a folded structure and maintain it.
    This is one in a series of videos looking at the chemistry of amino acids and proteins. Other in the series look at: the structures of amino acids; the zwitterion and its amphoteric properties; the reactions of the amino acid glycine (2-aminoethanoic acid) with sodium hydroxide, sodium carbonate and aqueous copper (II) sulfate solution; formation of two different dipeptides by the condensation reactions of glycine and alanine; formation of the backbone structure of a polypeptide; fibrous proteins verses globular proteins; protein hydrolysis

Komentáře • 3