Luokat: Kaikki - polar - attraction - ionic - hydrogen

jonka Osalumese Ikpotokin 14 tuntia sitten

16

Biological Molecules and Intermolecular Forces

Intermolecular forces play a crucial role in determining the physical properties of substances. Dispersion forces, the weakest type, occur when electrons in adjacent atoms form temporary dipoles.

Biological Molecules and Intermolecular Forces

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Biological Molecules and Intermolecular Forces

DIPOLE-DIPOLE

The attraction between the partially negative end of one polar molecule and the partially positive end of a different polar molecule.
• Stronger than London forces • Hold polar molecules to one anothe • Between polar molecules, influencing protein folding

DISPERSION

Examples
A temporary attractive force that results when the electrons in two adjacent atoms occupy positions that make the atoms form temporary dipoles.
• The weakest intermolecular force.
• Present in lipid bilayer
• Only forces that hold nonpolar molecules to one another
• Exist between all atoms and molecules. • Helium, and small nonpolar molecules, such as methane, CH 4(g) (in natural gas) which is why these materials are gases at room temperature

HYDROGEN BONDING

Example
Definition
A strong type of dipole interaction that happens when hydrogen (H) is bonded to nitrogen (N) or oxygen (O).
• Between polar molecules containing N, O, or F • Accounts for the properties of water: high solubility of polar and ionic substances, cohesion, adhesion, high surface tension, capillarity, high specific heat capacity, and high specific heat of vaporization. • Hydrogen bonding within proteins in spider silk contributes to its strength.

IONIC DIPOLE

Example
Definition
When a charged ion is attracted to a polar molecule. The polar molecule has a partially charged side, which pulls on the oppositely charged ion.
Facts/Characteristics
• Stronger than dipole-dipole interactions • Electrostatic attraction between oppositely charged ions. • Holds ions together in salt (NaCl) • Contributes to enzyme active sites and protein stability.