Hydrogen bonds

Definition

Hydrogen bonds are weak interactions that occur when a hydrogen atom covalently bonded to a highly electronegative atom is attracted to another electronegative atom. These bonds play a crucial role in the structure and function of proteins.

5 Must Know Facts For Your Next Test

1. Hydrogen bonds stabilize protein secondary structures such as alpha-helices and beta-sheets.
2. They are weaker than covalent bonds but significantly contribute to the overall stability of protein molecules.
3. Hydrogen bonding between amino acid residues helps maintain the three-dimensional shape of proteins.
4. Disruption of hydrogen bonds can lead to protein denaturation, affecting its function.
5. In aqueous environments, hydrogen bonds also interact with water molecules, influencing protein solubility.

Review Questions

• How do hydrogen bonds contribute to the secondary structure of proteins?
• What is the impact of disrupting hydrogen bonds on protein function?
• Why are hydrogen bonds important in maintaining the three-dimensional shape of proteins?

Related terms

Covalent Bond: A strong bond formed by sharing electrons between atoms.

Denaturation:

The process where proteins lose their structure and function due to external stress or compounds.

Amino Acid Residue: The remaining part of an amino acid after it has been incorporated into a peptide or protein chain.