4 terms

Definition: A hydrogen atom bound to a strongly electronegative atom (such as nitrogen or oxygen) exhibits a significant dipole-dipole interaction.

Example: Essential for protein folding and DNA structure, which keeps base pairs together.

More detail: Vital to preserving biomolecules' functionality and structure.

Note: Water's special qualities, like its high boiling point and surface tension, are caused by hydrogen bonding.

Definition: Interactions between functional groups or ions that are negatively and positively charged.

Example: contributes to the interactions between enzymes and substrates and stabilizes protein structures.

More Detail: The strongest of the four varieties, although because it is polar, it may become weaker in water.

Notes: Ionic bonds support the stability of intricate molecular structures and are necessary for the creation of salt bridges in proteins.

Definition: Weak, temporary pressures brought on by molecules' electron motion.

Example: Help in maintaining both lipid bilayers' and proteins' strength in cell membranes.

More details: All molecules include it, but non-polar molecules especially need it.

Notes: When a lot of molecules are present, dispersion forces, despite their weakness, can add up to meaningful interactions.

Definition: Polar molecules having partial positive and partial negative charges are attracted to one another.

Example: Crucial to the interactions between polar protein domains and water molecules.

More Details: Weaker than ionic contacts and hydrogen bonds but stronger than dispersion forces.

Notes: The solubility of molecules in water and other polar solvents is influenced by these interactions.