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Hydrophobic Interactions van der Waals Forces

Secondary, tertiary, and quaternary structures of a protein are mainly stabilized by hydrophobic interactions, van der Waals forces, and by hydrogen bonds. [Pg.351]

The other major approach to making a microfluidic bioreactor is to use non-covalent techniques. One non-covalent approach involves non-specific adsorption of a biomolecule to the sohd support in the hioreactor [4]. This relies on the non-specific physical adsorption of the protein to the surface of the sohd support within the microfluidic device. This binding rehes on forces such as hydrogen bonding, ionic interactions, hydrophobic interactions, van der Waals forces and so on. Because there is no chemical reaction, the bioactive molecule is not changed and it can therefore retain its full activity for use... [Pg.1149]

See other pages where Hydrophobic Interactions van der Waals Forces is mentioned: [Pg.56]    [Pg.356]    [Pg.128]    [Pg.415]    [Pg.209]    [Pg.1014]    [Pg.235]    [Pg.215]    [Pg.33]    [Pg.33]    [Pg.43]    [Pg.199]    [Pg.68]    [Pg.200]    [Pg.26]    [Pg.254]    [Pg.1873]    [Pg.25]    [Pg.3350]    [Pg.942]    [Pg.166]    [Pg.285]    [Pg.1727]   


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Force hydrophobic interaction

Hydrophobic force

Hydrophobic interactions

Hydrophobic/hydrophobicity interactions

Hydrophobized interaction

Interaction force

Interaction van der Waals

Van der Waal forces

Van der Waal interactions

Van der Waals forces

Van der Waals, forces interactions

Van forces

Waals interactions

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