Hydrogen bonds are the strongest of the intermolecular forces. However, that strength is little in comparison the strength of intramolecular forces, such as ionic and covalent bonds. The strongest of the listed forces is covalent bonds, followed by ionic bonds, hydrogen bonds, and then finally London dispersion forces.

Hydrogen bonds are important in biochemistry because of the incredible effect that they have on life due to their relative strength. But remember, this strength is not nearly as as strong as the covalent and ionic bonds, which actually hold atoms within the same molecule together.

Note, hydrogen bonds can be either an intermolecular or an intramolecular force. A hydrogen bond is considered intramolecular if it is occurring between different molecules, and intermolecular if it is occurring within the same molecule.

Hydrogen bonds are the strongest of the intermolecular forces. However, that strength is little in comparison the strength of intramolecular forces, such as ionic and covalent bonds. The strongest of the listed forces is covalent bonds, followed by ionic bonds, hydrogen bonds, and then finally London dispersion forces.

Hydrogen bonds are important in biochemistry because of the incredible effect that they have on life due to their relative strength. But remember, this strength is not nearly as as strong as the covalent and ionic bonds, which actually hold atoms within the same molecule together.

Note, hydrogen bonds can be either an intermolecular or an intramolecular force. A hydrogen bond is considered intramolecular if it is occurring between different molecules, and intermolecular if it is occurring within the same molecule.

A polar molecule has both positive and negative ends. This dipole can interact in many ways with other molecules, both polar and non-polar. If it interacts with a neighboring nonpolar molecule, there is an induced dipole within that neighbor resulting in a dipole-induced dipole force.

A polar molecule has both positive and negative ends. This dipole can interact in many ways with other molecules, both polar and non-polar. If it interacts with a neighboring nonpolar molecule, there is an induced dipole within that neighbor resulting in a dipole-induced dipole force.

Biomolecules contain carbon as their key element, and they mostly contain nonmetallic elements. For example, the human body is about 65% oxygen, 20% carbon, 10% hydrogen, and 3% nitrogen - the remaining major elements that make up the human body are calcium, phosphorous, magnesium, sulfur, potassium, sodium, chlorine, and other trace elements like iron and copper. Ionic bonds are rare in biomolecules, as most biomolecules are bound via covalent bonds. Also, to create a specific biomolecule, many of the bonds must be in specific orientations-specific stereoisomers are important, especially with enzymes.

Biomolecules contain carbon as their key element, and they mostly contain nonmetallic elements. For example, the human body is about 65% oxygen, 20% carbon, 10% hydrogen, and 3% nitrogen - the remaining major elements that make up the human body are calcium, phosphorous, magnesium, sulfur, potassium, sodium, chlorine, and other trace elements like iron and copper. Ionic bonds are rare in biomolecules, as most biomolecules are bound via covalent bonds. Also, to create a specific biomolecule, many of the bonds must be in specific orientations-specific stereoisomers are important, especially with enzymes.

Hydrophobic effects require water to occur. The reason that hydrophobic groups tend to group together is that by doing so, the network of water molecules around them stays intact. There are no other special forces at play between hydrophobic groups. It is precisely the non-polar nature of hydrophobic groups that gives them their character; water molecules are polar. Cell membranes have a phospholipid bilayer with internal hydrophobic regions (the lipid tails), holding together the membrane.

Proteins will behave similarly to phospholipids in water; the polar groups will form favorable interactions on the surface with water, while the hydrophobic groups will be in the core and away from the water molecules. Usually, amino acids with non-polar residues will be found in the core of proteins. Tryptophan has a nonpolar side chain, and will thus be found in the core of a protein that is in a aqueous environment.

Hydrophobic effects require water to occur. The reason that hydrophobic groups tend to group together is that by doing so, the network of water molecules around them stays intact. There are no other special forces at play between hydrophobic groups. It is precisely the non-polar nature of hydrophobic groups that gives them their character; water molecules are polar. Cell membranes have a phospholipid bilayer with internal hydrophobic regions (the lipid tails), holding together the membrane.

Proteins will behave similarly to phospholipids in water; the polar groups will form favorable interactions on the surface with water, while the hydrophobic groups will be in the core and away from the water molecules. Usually, amino acids with non-polar residues will be found in the core of proteins. Tryptophan has a nonpolar side chain, and will thus be found in the core of a protein that is in a aqueous environment.