Sandbox108: Difference between revisions

Tertiary structure of protein is characterized by the “global” folding of a polypeptide chain. [http://www.stanford.edu/group/pandegroup/folding/education/prstruc.html] Hydrophobic interaction is a major driving force determining the tertiary structure of the proteins. [http://www.stanford.edu/group/pandegroup/folding/education/prstruc.html] The reason why hydrophobic interaction is important is because of relationship with the hydrogen bonding. The peptide backbone is hydrophilic, but in the middle of proteins is mostly in a hydrophobic circumstance. So, in order to reduce the hydrophilicity, to maximize the hydrogen bonding, the α-helix <show α-helix wiki text> and the β-sheet <show the β-sheet wiki text> can break down the C=O and N-H groups in the peptide bonds so that the hydrogen bonds are maximum. [http://www.massey.ac.nz/~wwbioch/Prot/thirds/framset.htm] Also, all polar and hydrophilic side chains interact with H-bonds. Hydrogen bonding <show the H.B wiki text> is crucial in stabilizing the tertiary structure. [http://webhost.bridgew.edu/fgorga/proteins/proteins.htm] On the other hand, disulfide bonds <show the disulfide bonds of cysteine wiki text> between cysteine residues stabilize the tertiary structure. [http://webhost.bridgew.edu/fgorga/proteins/proteins.htm]