nonpolar molecules
Ni, just peptide bonding. Hydrophobic interactions do not have significance to folding until tertiary structure folding.
lipid bilayer of cell membrane
Hydrophobic interactions cause proteins to form into a three-dimensional shape.
By simply afecting the bonds ( hbonds . ionic bonds and hydrophobic interactions )
All receptors - both intra- and extra- cellular - are extremely specific in their interactions.
An example of the protein-protein interactions is the antigen-antibody interactions. Because of the complexity of the protein molecules, the hydrophobic interactions are more dominant.
Ni, just peptide bonding. Hydrophobic interactions do not have significance to folding until tertiary structure folding.
non covalent
Hydrophobic interactions are repulsive and hydrogen bonds are attractive forces. So, not sure hydrophobic interaction is classified as a "force" but rather and "interaction". Hydrogen bonds are relatively strong forces. It's really difficult to compare hydrophobic interaction with hydrogen bond because they are sort of opposite.
between two charged molecules
lipid bilayer of cell membrane
By simply afecting the bonds ( hbonds . ionic bonds and hydrophobic interactions )
Four of them are; hydrophobic and hydrophilic interactions, hydrogen bonding and disulphide bridging.
By simply afecting the bonds ( hbonds . ionic bonds and hydrophobic interactions )
Hydrophobic interactions cause proteins to form into a three-dimensional shape.
hydrophobic interactions
All receptors - both intra- and extra- cellular - are extremely specific in their interactions.